BASI_HUMAN
ID BASI_HUMAN Reviewed; 385 AA.
AC P35613; A6NJW1; D3YLG5; Q7Z796; Q8IZL7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 226.
DE RecName: Full=Basigin {ECO:0000305};
DE AltName: Full=5F7;
DE AltName: Full=Collagenase stimulatory factor;
DE AltName: Full=Extracellular matrix metalloproteinase inducer;
DE Short=EMMPRIN;
DE AltName: Full=Hepatoma-associated antigen {ECO:0000303|PubMed:15688292};
DE Short=HAb18G {ECO:0000303|PubMed:15688292};
DE AltName: Full=Leukocyte activation antigen M6;
DE AltName: Full=OK blood group antigen;
DE AltName: Full=Tumor cell-derived collagenase stimulatory factor;
DE Short=TCSF;
DE AltName: CD_antigen=CD147;
DE Flags: Precursor;
GN Name=BSG {ECO:0000312|HGNC:HGNC:1116}; ORFNames=UNQ6505/PRO21383;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=1634773;
RA Kasinrerk W., Fiebiger E., Stefanova I., Baumruker T., Knapp W.,
RA Stockinger H.;
RT "Human leukocyte activation antigen M6, a member of the Ig superfamily, is
RT the species homologue of rat OX-47, mouse basigin, and chicken HT7
RT molecule.";
RL J. Immunol. 149:847-854(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RX PubMed=1783610; DOI=10.1093/oxfordjournals.jbchem.a123657;
RA Miyauchi T., Masuzawa Y., Muramatsu T.;
RT "The basigin group of the immunoglobulin superfamily: complete conservation
RT of a segment in and around transmembrane domains of human and mouse basigin
RT and chicken HT7 antigen.";
RL J. Biochem. 110:770-774(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=7812975;
RA Biswas C., Zhang Y., Decastro R., Guo H., Nakamura T., Kataoka H.,
RA Nabeshima K.;
RT "The human tumor cell-derived collagenase stimulatory factor (renamed
RT EMMPRIN) is a member of the immunoglobulin superfamily.";
RL Cancer Res. 55:434-439(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA Wakasugi H., Scamps C., Yang G., Vancong N., Bernheim A., Tursz T.,
RA Harada N.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA Decastro R., Zhang Y., Kataoka H., Coon J., Biswas C.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RX PubMed=9767135; DOI=10.1016/s0378-1119(98)00400-4;
RA Guo H., Majmudar G., Jensen T.C., Biswas C., Toole B.P., Gordon M.K.;
RT "Characterization of the gene for human EMMPRIN, a tumor cell surface
RT inducer of matrix metalloproteinases.";
RL Gene 220:99-108(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA Sato T., Takita M., Noguchi Y., Hirata M., Sakai T., Ito A.;
RT "Regulation of EMMPRIN/CD147 expression and its function of controlling
RT matrix metalloproteinases production and cell-surface localization in co-
RT culture of human uterine cervical carcinoma SKG-II cells and human uterine
RT cervical fibroblasts.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA Kim D., Kanai Y., Choi H., Shin H., Kim J., Teraoka H., Shigeta Y.,
RA Chairoungdua A., Babu E., Anzai N., Iribe Y., Endou H.;
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=12939332; DOI=10.1167/iovs.02-0995;
RA Ochrietor J.D., Moroz T.P., van Ekeris L., Clamp M.F., Jefferson S.C.,
RA deCarvalho A.C., Fadool J.M., Wistow G., Muramatsu T., Linser P.J.;
RT "Retina-specific expression of 5A11/Basigin-2, a member of the
RT immunoglobulin gene superfamily.";
RL Invest. Ophthalmol. Vis. Sci. 44:4086-4096(2003).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), SUBUNIT (ISOFORMS 2 AND 3),
RP SUBCELLULAR LOCATION (ISOFORMS 2; 3 AND 4), ALTERNATIVE PROMOTER USAGE,
RP TISSUE SPECIFICITY (ISOFORMS 2; 3 AND 4), AND GLYCOSYLATION (ISOFORMS 2; 3
RP AND 4).
RX PubMed=21536654; DOI=10.1128/mcb.05160-11;
RA Liao C.G., Kong L.M., Song F., Xing J.L., Wang L.X., Sun Z.J., Tang H.,
RA Yao H., Zhang Y., Wang L., Wang Y., Yang X.M., Li Y., Chen Z.N.;
RT "Characterization of basigin isoforms and the inhibitory function of
RT basigin-3 in human hepatocellular carcinoma proliferation and invasion.";
RL Mol. Cell. Biol. 31:2591-2604(2011).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [16]
RP PROTEIN SEQUENCE OF 22-36 (ISOFORM 1).
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [17]
RP PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX PubMed=1846736; DOI=10.1016/0003-9861(91)90332-d;
RA Nabeshima K., Lane W.S., Biswas C.;
RT "Partial sequencing and characterization of the tumor cell-derived
RT collagenase stimulatory factor.";
RL Arch. Biochem. Biophys. 285:90-96(1991).
RN [18]
RP FUNCTION (ISOFORM 2).
RX PubMed=11688976; DOI=10.1006/bbrc.2001.5847;
RA Yurchenko V., O'Connor M., Dai W.W., Guo H., Toole B., Sherry B.,
RA Bukrinsky M.;
RT "CD147 is a signaling receptor for cyclophilin B.";
RL Biochem. Biophys. Res. Commun. 288:786-788(2001).
RN [19]
RP FUNCTION (ISOFORM 2) (MICROBIAL INFECTION), AND INTERACTION WITH PPIA
RP (ISOFORM 2).
RX PubMed=11353871; DOI=10.1073/pnas.111583198;
RA Pushkarsky T., Zybarth G., Dubrovsky L., Yurchenko V., Tang H., Guo H.,
RA Toole B., Sherry B., Bukrinsky M.;
RT "CD147 facilitates HIV-1 infection by interacting with virus-associated
RT cyclophilin A.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6360-6365(2001).
RN [20]
RP FUNCTION (ISOFORM 2).
RX PubMed=12553375; DOI=10.1023/a:1021350718226;
RA Caudroy S., Polette M., Nawrocki-Raby B., Cao J., Toole B.P., Zucker S.,
RA Birembaut P.;
RT "EMMPRIN-mediated MMP regulation in tumor and endothelial cells.";
RL Clin. Exp. Metastasis 19:697-702(2002).
RN [21]
RP FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), AND TISSUE
RP SPECIFICITY (ISOFORM 2).
RX PubMed=11992541; DOI=10.1002/ijc.10390;
RA Kanekura T., Chen X., Kanzaki T.;
RT "Basigin (CD147) is expressed on melanoma cells and induces tumor cell
RT invasion by stimulating production of matrix metalloproteinases by
RT fibroblasts.";
RL Int. J. Cancer 99:520-528(2002).
RN [22]
RP FUNCTION (ISOFORM 2), MUTAGENESIS (ISOFORM 2), AND INTERACTION WITH PPIA
RP (ISOFORM 2).
RX PubMed=11943775; DOI=10.1074/jbc.m201593200;
RA Yurchenko V., Zybarth G., O'Connor M., Dai W.W., Franchin G., Hao T.,
RA Guo H., Hung H.C., Toole B., Gallay P., Sherry B., Bukrinsky M.;
RT "Active site residues of cyclophilin A are crucial for its signaling
RT activity via CD147.";
RL J. Biol. Chem. 277:22959-22965(2002).
RN [23]
RP REVIEW.
RX PubMed=12792908; DOI=10.14670/hh-18.981;
RA Muramatsu T., Miyauchi T.;
RT "Basigin (CD147): a multifunctional transmembrane protein involved in
RT reproduction, neural function, inflammation and tumor invasion.";
RL Histol. Histopathol. 18:981-987(2003).
RN [24]
RP GLYCOSYLATION AT ASN-160 AND ASN-268.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [25]
RP FUNCTION (ISOFORM 2).
RX PubMed=15833850; DOI=10.1158/0008-5472.can-04-3605;
RA Tang Y., Nakada M.T., Kesavan P., McCabe F., Millar H., Rafferty P.,
RA Bugelski P., Yan L.;
RT "Extracellular matrix metalloproteinase inducer stimulates tumor
RT angiogenesis by elevating vascular endothelial cell growth factor and
RT matrix metalloproteinases.";
RL Cancer Res. 65:3193-3199(2005).
RN [26]
RP FUNCTION (ISOFORM 2) (MICROBIAL INFECTION), INTERACTION WITH PPIA (ISOFORM
RP 2), AND SUBCELLULAR LOCATION (ISOFORM 2).
RX PubMed=15688292; DOI=10.1086/427811;
RA Chen Z., Mi L., Xu J., Yu J., Wang X., Jiang J., Xing J., Shang P.,
RA Qian A., Li Y., Shaw P.X., Wang J., Duan S., Ding J., Fan C., Zhang Y.,
RA Yang Y., Yu X., Feng Q., Li B., Yao X., Zhang Z., Li L., Xue X., Zhu P.;
RT "Function of HAb18G/CD147 in invasion of host cells by severe acute
RT respiratory syndrome coronavirus.";
RL J. Infect. Dis. 191:755-760(2005).
RN [27]
RP INTERACTION WITH PPIL2 (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), AND
RP MUTAGENESIS (ISOFORM 2).
RX PubMed=15946952; DOI=10.1074/jbc.m503770200;
RA Pushkarsky T., Yurchenko V., Vanpouille C., Brichacek B., Vaisman I.,
RA Hatakeyama S., Nakayama K.I., Sherry B., Bukrinsky M.I.;
RT "Cell surface expression of CD147/EMMPRIN is regulated by cyclophilin 60.";
RL J. Biol. Chem. 280:27866-27871(2005).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [29]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [30]
RP FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), AND INTERACTION
RP WITH SLC16A1 (ISOFORM 2).
RX PubMed=17127621; DOI=10.1080/09687860600841967;
RA Manoharan C., Wilson M.C., Sessions R.B., Halestrap A.P.;
RT "The role of charged residues in the transmembrane helices of
RT monocarboxylate transporter 1 and its ancillary protein basigin in
RT determining plasma membrane expression and catalytic activity.";
RL Mol. Membr. Biol. 23:486-498(2006).
RN [31]
RP INTERACTION WITH AJAP1 (ISOFORM 2), AND SUBCELLULAR LOCATION (ISOFORM 2).
RX PubMed=17267690; DOI=10.1091/mbc.e06-07-0637;
RA Schreiner A., Ruonala M., Jakob V., Suthaus J., Boles E., Wouters F.,
RA Starzinski-Powitz A.;
RT "junction protein shrew-1 influences cell invasion and interacts with
RT invasion-promoting protein CD147.";
RL Mol. Biol. Cell 18:1272-1281(2007).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [33]
RP FUNCTION (ISOFORM 2).
RX PubMed=19837976; DOI=10.1182/blood-2009-04-217380;
RA Bougatef F., Quemener C., Kellouche S., Naimi B., Podgorniak M.P.,
RA Millot G., Gabison E.E., Calvo F., Dosquet C., Lebbe C., Menashi S.,
RA Mourah S.;
RT "EMMPRIN promotes angiogenesis through hypoxia-inducible factor-2alpha-
RT mediated regulation of soluble VEGF isoforms and their receptor VEGFR-2.";
RL Blood 114:5547-5556(2009).
RN [34]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160 AND ASN-268.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [35]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160 AND ASN-268.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [36]
RP FUNCTION (ISOFORM 2) (MICROBIAL INFECTION).
RX PubMed=20147391; DOI=10.1128/jvi.02168-09;
RA Watanabe A., Yoneda M., Ikeda F., Terao-Muto Y., Sato H., Kai C.;
RT "CD147/EMMPRIN acts as a functional entry receptor for measles virus on
RT epithelial cells.";
RL J. Virol. 84:4183-4193(2010).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [38]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [39]
RP FUNCTION (ISOFORM 2), AND INTERACTION WITH SLC16A12 (ISOFORM 2).
RX PubMed=21778275; DOI=10.1167/iovs.10-6579;
RA Castorino J.J., Gallagher-Colombo S.M., Levin A.V., Fitzgerald P.G.,
RA Polishook J., Kloeckener-Gruissem B., Ostertag E., Philp N.J.;
RT "Juvenile cataract-associated mutation of solute carrier SLC16A12 impairs
RT trafficking of the protein to the plasma membrane.";
RL Invest. Ophthalmol. Vis. Sci. 52:6774-6784(2011).
RN [40]
RP INTERACTION WITH PPIA.
RX PubMed=21245143; DOI=10.1074/jbc.c110.181347;
RA Song F., Zhang X., Ren X.B., Zhu P., Xu J., Wang L., Li Y.F., Zhong N.,
RA Ru Q., Zhang D.W., Jiang J.L., Xia B., Chen Z.N.;
RT "Cyclophilin A (CyPA) induces chemotaxis independent of its peptidylprolyl
RT cis-trans isomerase activity: direct binding between CyPA and the
RT ectodomain of CD147.";
RL J. Biol. Chem. 286:8197-8203(2011).
RN [41]
RP FUNCTION (ISOFORMS 1 AND 2) (MICROBIAL INFECTION), INTERACTION WITH
RP P.FALCIPARUM RH5 (ISOFORMS 1 AND 2) (MICROBIAL INFECTION), GLYCOSYLATION,
RP VARIANTS ASN-152; LEU-176; PRO-206; LYS-208 AND VAL-269, AND MUTAGENESIS OF
RP ASN-160; ASN-268 AND ASN-302.
RX PubMed=22080952; DOI=10.1038/nature10606;
RA Crosnier C., Bustamante L.Y., Bartholdson S.J., Bei A.K., Theron M.,
RA Uchikawa M., Mboup S., Ndir O., Kwiatkowski D.P., Duraisingh M.T.,
RA Rayner J.C., Wright G.J.;
RT "Basigin is a receptor essential for erythrocyte invasion by Plasmodium
RT falciparum.";
RL Nature 480:534-537(2011).
RN [42]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [43]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [44]
RP INTERACTION WITH P.FALCIPARUM RH5 (ISOFORM 2) (MICROBIAL INFECTION), AND
RP MUTAGENESIS OF (ISOFORM 2).
RX PubMed=24297912; DOI=10.1073/pnas.1320771110;
RA Wanaguru M., Liu W., Hahn B.H., Rayner J.C., Wright G.J.;
RT "RH5-Basigin interaction plays a major role in the host tropism of
RT Plasmodium falciparum.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20735-20740(2013).
RN [45]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362 AND SER-368, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [46]
RP FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1), TISSUE SPECIFICITY
RP (ISOFORM 1), AND INTERACTION WITH NXNL1 (ISOFORM 1).
RX PubMed=25957687; DOI=10.1016/j.cell.2015.03.023;
RA Ait-Ali N., Fridlich R., Millet-Puel G., Clerin E., Delalande F.,
RA Jaillard C., Blond F., Perrocheau L., Reichman S., Byrne L.C.,
RA Olivier-Bandini A., Bellalou J., Moyse E., Bouillaud F., Nicol X.,
RA Dalkara D., van Dorsselaer A., Sahel J.A., Leveillard T.;
RT "Rod-derived cone viability factor promotes cone survival by stimulating
RT aerobic glycolysis.";
RL Cell 161:817-832(2015).
RN [47]
RP FUNCTION (ISOFORM 2) (MICROBIAL INFECTION), INTERACTION WITH P.FACILPARUM
RP RH5 (ISOFORM 2)(MICROBIAL INFECTION), SUBCELLULAR LOCATION (ISOFORM 2),
RP TISSUE SPECIFICITY (ISOFORM 2), AND BIOTECHNOLOGY (ISOFORM 2).
RX PubMed=26195724; DOI=10.1084/jem.20150032;
RA Zenonos Z.A., Dummler S.K., Mueller-Sienerth N., Chen J., Preiser P.R.,
RA Rayner J.C., Wright G.J.;
RT "Basigin is a druggable target for host-oriented antimalarial
RT interventions.";
RL J. Exp. Med. 212:1145-1151(2015).
RN [48]
RP FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), INTERACTION WITH
RP VEGFA AND VEGFR2 (ISOFORM 2), MUTAGENESIS (ISOFORM 2), AND REGION (ISOFORM
RP 2).
RX PubMed=25825981; DOI=10.18632/oncotarget.2870;
RA Khayati F., Perez-Cano L., Maouche K., Sadoux A., Boutalbi Z.,
RA Podgorniak M.P., Maskos U., Setterblad N., Janin A., Calvo F., Lebbe C.,
RA Menashi S., Fernandez-Recio J., Mourah S.;
RT "EMMPRIN/CD147 is a novel coreceptor of VEGFR-2 mediating its activation by
RT VEGF.";
RL Oncotarget 6:9766-9780(2015).
RN [49]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [50]
RP INTERACTION WITH XKR8.
RX PubMed=27503893; DOI=10.1073/pnas.1610403113;
RA Suzuki J., Imanishi E., Nagata S.;
RT "Xkr8 phospholipid scrambling complex in apoptotic phosphatidylserine
RT exposure.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9509-9514(2016).
RN [51]
RP FUNCTION (ISOFORM 2), AND INTERACTION WITH SLC16A11 (ISOFORM 2).
RX PubMed=28666119; DOI=10.1016/j.cell.2017.06.011;
RG MEDIA Consortium;
RG SIGMA T2D Consortium;
RA Rusu V., Hoch E., Mercader J.M., Tenen D.E., Gymrek M., Hartigan C.R.,
RA DeRan M., von Grotthuss M., Fontanillas P., Spooner A., Guzman G.,
RA Deik A.A., Pierce K.A., Dennis C., Clish C.B., Carr S.A., Wagner B.K.,
RA Schenone M., Ng M.C.Y., Chen B.H., Centeno-Cruz F., Zerrweck C., Orozco L.,
RA Altshuler D.M., Schreiber S.L., Florez J.C., Jacobs S.B.R., Lander E.S.;
RT "Type 2 diabetes variants disrupt function of SLC16A11 through two distinct
RT mechanisms.";
RL Cell 170:199-212(2017).
RN [52]
RP FUNCTION (ISOFORM 2) (MICROBIAL INFECTION), SUBCELLULAR LOCATION (ISOFORM
RP 2), AND TISSUE SPECIFICITY (ISOFORM 2).
RX PubMed=28409866; DOI=10.1111/cmi.12747;
RA Aniweh Y., Gao X., Hao P., Meng W., Lai S.K., Gunalan K., Chu T.T.,
RA Sinha A., Lescar J., Chandramohanadas R., Li H.Y., Sze S.K., Preiser P.R.;
RT "P. falciparum RH5-Basigin interaction induces changes in the cytoskeleton
RT of the host RBC.";
RL Cell. Microbiol. 19:0-0(2017).
RN [53]
RP FUNCTION (MICROBIAL INFECTION) (ISOFORM 2), AND SUBCELLULAR LOCATION
RP (ISOFORM 2).
RX PubMed=29739904; DOI=10.1128/mbio.00781-18;
RA Vanarsdall A.L., Pritchard S.R., Wisner T.W., Liu J., Jardetzky T.S.,
RA Johnson D.C.;
RT "CD147 Promotes Entry of Pentamer-Expressing Human Cytomegalovirus into
RT Epithelial and Endothelial Cells.";
RL MBio 9:0-0(2018).
RN [54]
RP REVIEW ON FUNCTION (MICROBIAL FUNCTION), AND REVIEW ON INTERACTION WITH
RP SARS-COV-2 SPIKE GLYCOPROTEIN (MICROBIAL FUNCTION).
RX PubMed=32307653; DOI=10.1007/s12015-020-09976-7;
RA Ulrich H., Pillat M.M.;
RT "CD147 as a Target for COVID-19 Treatment: Suggested Effects of
RT Azithromycin and Stem Cell Engagement.";
RL Stem. Cell. Rev. Rep. 16:434-440(2020).
RN [55]
RP FUNCTION (MICROBIAL FUNCTION), AND INTERACTION WITH SARS-COV-2 SPIKE
RP GLYCOPROTEIN (MICROBIAL FUNCTION).
RX PubMed=33432067; DOI=10.1038/s41598-020-80464-1;
RA Shilts J., Crozier T.W.M., Greenwood E.J.D., Lehner P.J., Wright G.J.;
RT "No evidence for basigin/CD147 as a direct SARS-CoV-2 spike binding
RT receptor.";
RL Sci. Rep. 11:413-413(2021).
RN [56]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 140-321, SUBUNIT (ISOFORM 2), AND
RP DISULFIDE BONDS.
RX PubMed=18430721; DOI=10.1074/jbc.m802694200;
RA Yu X.-L., Hu T., Du J.-M., Ding J.-P., Yang X.-M., Zhang J., Yang B.,
RA Shen X., Zhang Z., Zhong W.-D., Wen N., Jiang H., Zhu P., Chen Z.-N.;
RT "Crystal structure of HAb18G/CD147: implications for immunoglobulin
RT superfamily homophilic adhesion.";
RL J. Biol. Chem. 283:18056-18065(2008).
RN [57]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 13-219, IDENTIFICATION BY MASS
RP SPECTROMETRY, SUBUNIT (ISOFORM 1), AND DISULFIDE BONDS.
RX PubMed=19768682; DOI=10.1002/prot.22577;
RA Luo J., Teplyakov A., Obmolova G., Malia T., Wu S.-J., Beil E., Baker A.,
RA Swencki-Underwood B., Zhao Y., Sprenkle J., Dixon K., Sweet R.,
RA Gilliland G.L.;
RT "Structure of the EMMPRIN N-terminal domain 1: dimerization via beta-strand
RT swapping.";
RL Proteins 77:1009-1014(2009).
RN [58] {ECO:0007744|PDB:3QQN, ECO:0007744|PDB:3QR2}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 23-138, FUNCTION (ISOFORM 1),
RP DISULFIDE BOND, AND MUTAGENESIS OF CYS-67.
RX PubMed=21620857; DOI=10.1016/j.jmb.2011.04.060;
RA Redzic J.S., Armstrong G.S., Isern N.G., Jones D.N., Kieft J.S.,
RA Eisenmesser E.Z.;
RT "The retinal specific CD147 Ig0 domain: from molecular structure to
RT biological activity.";
RL J. Mol. Biol. 411:68-82(2011).
RN [59] {ECO:0007744|PDB:4U0Q}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 140-385, INTERACTION WITH
RP P.FACILPARUM RH5 (ISOFORM 2) (MICROBIAL INFECTION), AND DISULFIDE BONDS.
RX PubMed=25132548; DOI=10.1038/nature13715;
RA Wright K.E., Hjerrild K.A., Bartlett J., Douglas A.D., Jin J., Brown R.E.,
RA Illingworth J.J., Ashfield R., Clemmensen S.B., de Jongh W.A., Draper S.J.,
RA Higgins M.K.;
RT "Structure of malaria invasion protein RH5 with erythrocyte basigin and
RT blocking antibodies.";
RL Nature 515:427-430(2014).
RN [60] {ECO:0007744|PDB:5X0T}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 138-217, AND DISULFIDE BONDS.
RA Zhang M.-Y., Lin P., Zhu P., Chen Z.-N.;
RT "Crystal structure of CD147 C2 domain in complex with Fab of its monoclonal
RT antibody.";
RL Submitted (JAN-2017) to the PDB data bank.
RN [61]
RP VARIANT LYS-208.
RX PubMed=9130641; DOI=10.1002/eji.1830270414;
RA Spring F.A., Holmes C.H., Simpson K.L., Mawby W.J., Mattes M.J., Okubo Y.,
RA Parsons S.F.;
RT "The Ok(a) blood group antigen is a marker for the M6 leukocyte activation
RT antigen, the human homolog of OX-47 antigen, basigin and neurothelin, an
RT immunoglobulin superfamily molecule that is widely expressed in human cells
RT and tissues.";
RL Eur. J. Immunol. 27:891-897(1997).
RN [62]
RP VARIANTS VAL-13; ALA-16 AND PHE-26.
RX PubMed=32867305; DOI=10.3390/genes11091010;
RA Latini A., Agolini E., Novelli A., Borgiani P., Giannini R., Gravina P.,
RA Smarrazzo A., Dauri M., Andreoni M., Rogliani P., Bernardini S.,
RA Helmer-Citterich M., Biancolella M., Novelli G.;
RT "COVID-19 and Genetic Variants of Protein Involved in the SARS-CoV-2 Entry
RT into the Host Cells.";
RL Genes (Basel) 11:0-0(2020).
CC -!- FUNCTION: [Isoform 1]: Essential for normal retinal maturation and
CC development (By similarity). Acts as a retinal cell surface receptor
CC for NXNL1 and plays an important role in NXNL1-mediated survival of
CC retinal cone photoreceptors (PubMed:25957687). In association with
CC glucose transporter SLC16A1/GLUT1 and NXNL1, promotes retinal cone
CC survival by enhancing aerobic glycolysis and accelerating the entry of
CC glucose into photoreceptors (PubMed:25957687). May act as a potent
CC stimulator of IL6 secretion in multiple cell lines that include
CC monocytes (PubMed:21620857). {ECO:0000250|UniProtKB:P18572,
CC ECO:0000269|PubMed:21620857, ECO:0000269|PubMed:25957687}.
CC -!- FUNCTION: [Isoform 1]: (Microbial infection) Erythrocyte receptor for
CC P.falciparum RH5 which is essential for erythrocyte invasion by the
CC merozoite stage of P.falciparum isolates 3D7 and Dd2.
CC {ECO:0000269|PubMed:22080952}.
CC -!- FUNCTION: [Isoform 2]: Signaling receptor for cyclophilins, essential
CC for PPIA/CYPA and PPIB/CYPB-dependent signaling related to chemotaxis
CC and adhesion of immune cells (PubMed:11943775, PubMed:11688976). Plays
CC an important role in targeting monocarboxylate transporters
CC SLC16A1/GLUT1, SLC16A11 and SLC16A12 to the plasma membrane
CC (PubMed:17127621, PubMed:21778275, PubMed:28666119). Acts as a
CC coreceptor for vascular endothelial growth factor receptor 2
CC (KDR/VEGFR2) in endothelial cells enhancing its VEGFA-mediated
CC activation and downstream signaling (PubMed:25825981). Promotes
CC angiogenesis through EPAS1/HIF2A-mediated up-regulation of VEGFA
CC (isoform VEGF-165 and VEGF-121) and KDR/VEGFR2 in endothelial cells
CC (PubMed:19837976). Plays a key role in regulating tumor growth,
CC invasion, metastasis and neoangiogenesis by stimulating the production
CC and release of extracellular matrix metalloproteinases and KDR/VEGFR2
CC by both tumor cells and stromal cells (fibroblasts and endothelial
CC cells) (PubMed:12553375, PubMed:11992541, PubMed:15833850).
CC {ECO:0000269|PubMed:11688976, ECO:0000269|PubMed:11943775,
CC ECO:0000269|PubMed:11992541, ECO:0000269|PubMed:12553375,
CC ECO:0000269|PubMed:15833850, ECO:0000269|PubMed:17127621,
CC ECO:0000269|PubMed:19837976, ECO:0000269|PubMed:21778275,
CC ECO:0000269|PubMed:25825981, ECO:0000269|PubMed:28666119}.
CC -!- FUNCTION: [Isoform 2]: (Microbial infection) Erythrocyte receptor for
CC P.falciparum RH5 which is essential for erythrocyte invasion by the
CC merozoite stage of P.falciparum isolates 3D7, Dd2, 7G8 and HB3
CC (PubMed:22080952, PubMed:26195724). Binding of P.falciparum RH5 results
CC in BSG dimerization which triggers an increase in intracellular Ca(2+)
CC in the erythrocyte (PubMed:28409866). This essential step leads to a
CC rearrangement of the erythrocyte cytoskeleton required for the
CC merozoite invasion (PubMed:28409866). {ECO:0000269|PubMed:22080952,
CC ECO:0000269|PubMed:26195724, ECO:0000269|PubMed:28409866}.
CC -!- FUNCTION: [Isoform 2]: (Microbial infection) Can facilitate human SARS
CC coronavirus (SARS-CoV-1) infection via its interaction with virus-
CC associated PPIA/CYPA. {ECO:0000269|PubMed:15688292}.
CC -!- FUNCTION: [Isoform 2]: (Microbial infection) Can facilitate HIV-1
CC infection via its interaction with virus-associated PPIA/CYPA.
CC {ECO:0000269|PubMed:11353871}.
CC -!- FUNCTION: [Isoform 2]: (Microbial infection) First described as a
CC receptor for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-
CC 2), it is not required for SARS-CoV-2 infection.
CC {ECO:0000269|PubMed:33432067, ECO:0000303|PubMed:32307653}.
CC -!- FUNCTION: [Isoform 2]: (Microbial infection) Acts as a receptor for
CC measles virus. {ECO:0000269|PubMed:20147391}.
CC -!- FUNCTION: [Isoform 2]: (Microbial infection) Promotes entry of
CC pentamer-expressing human cytomegalovirus (HCMV) into epithelial and
CC endothelial cells. {ECO:0000269|PubMed:29739904}.
CC -!- SUBUNIT: [Isoform 1]: Homooligomer (PubMed:19768682). Interacts with
CC NXNL1 (PubMed:25957687). Interacts with SLC2A1 and SLC16A1/GLUT1 (By
CC similarity). Interacts with XKR8; promoting its localization at the
CC cell membrane (PubMed:27503893). {ECO:0000250|UniProtKB:P17790,
CC ECO:0000269|PubMed:19768682, ECO:0000269|PubMed:25957687,
CC ECO:0000269|PubMed:27503893}.
CC -!- SUBUNIT: [Isoform 1]: (Microbial infection) Interacts with P.falciparum
CC (isolate 3D7) RH5/PfRH5; the interaction is required for the invasion
CC of the host erythrocytes by the parasite at the merozoite stage.
CC {ECO:0000269|PubMed:22080952}.
CC -!- SUBUNIT: [Isoform 2]: Homooligomer (PubMed:18430721). Forms
CC heterooligomers with isoform 3 (PubMed:21536654). Interacts with VEGFA
CC and KDR/VEGFR2 (PubMed:25825981). Interacts with PPIA/CYPA
CC (PubMed:11353871, PubMed:11943775, PubMed:15688292, PubMed:21245143).
CC Interacts with PPIL2; regulates BSG transport to the cell membrane
CC (PubMed:15946952). Interacts with SLC16A1/GLUT1 (PubMed:17127621).
CC Interacts with SLC16A12 (PubMed:21778275). Interacts with SLC16A11
CC (PubMed:28666119). Interacts with AJAP1 (PubMed:17267690). Interacts
CC with SLC1A3, ATP1B2, MAG and L1CAM (By similarity). Interacts with
CC SLC16A3; interaction mediates SLC16A3 targeting to the plasma membrane.
CC {ECO:0000250|UniProtKB:P18572, ECO:0000250|UniProtKB:P26453,
CC ECO:0000269|PubMed:11353871, ECO:0000269|PubMed:11943775,
CC ECO:0000269|PubMed:15688292, ECO:0000269|PubMed:15946952,
CC ECO:0000269|PubMed:17127621, ECO:0000269|PubMed:17267690,
CC ECO:0000269|PubMed:18430721, ECO:0000269|PubMed:21245143,
CC ECO:0000269|PubMed:21536654, ECO:0000269|PubMed:21778275,
CC ECO:0000269|PubMed:25825981, ECO:0000269|PubMed:28666119}.
CC -!- SUBUNIT: [Isoform 2]: (Microbial infection) Interacts with P.falciparum
CC (isolates 3D7 or 7G8) RH5/PfRH5; the interaction is required for the
CC invasion of the host erythrocytes by the parasite at the merozoite
CC stage. {ECO:0000269|PubMed:22080952, ECO:0000269|PubMed:24297912,
CC ECO:0000269|PubMed:25132548, ECO:0000269|PubMed:26195724}.
CC -!- SUBUNIT: [Isoform 2]: (Microbial infection) Does not interact with
CC severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike
CC glycoprotein, even if previous works were based on a putative
CC interaction. {ECO:0000269|PubMed:33432067,
CC ECO:0000303|PubMed:32307653}.
CC -!- SUBUNIT: [Isoform 3]: Forms heterooligomers with isoform 2.
CC {ECO:0000269|PubMed:21536654}.
CC -!- INTERACTION:
CC P35613; P05067: APP; NbExp=2; IntAct=EBI-750709, EBI-77613;
CC P35613; Q9UJC3: HOOK1; NbExp=3; IntAct=EBI-750709, EBI-746704;
CC P35613; Q92542: NCSTN; NbExp=6; IntAct=EBI-750709, EBI-998440;
CC P35613; P62937: PPIA; NbExp=2; IntAct=EBI-750709, EBI-437708;
CC P35613; PRO_0000025592 [P49768]: PSEN1; NbExp=6; IntAct=EBI-750709, EBI-2606356;
CC P35613; Q8NCK7: SLC16A11; NbExp=5; IntAct=EBI-750709, EBI-21840241;
CC P35613; P0DTC2: S; Xeno; NbExp=7; IntAct=EBI-750709, EBI-25474821;
CC P35613-2; Q13520: AQP6; NbExp=3; IntAct=EBI-11037868, EBI-13059134;
CC P35613-2; Q7RTY0: SLC16A13; NbExp=3; IntAct=EBI-11037868, EBI-12243266;
CC P35613-2; Q8IFM5: RH5; Xeno; NbExp=3; IntAct=EBI-11037868, EBI-22304327;
CC P35613-2; B2L3N7; Xeno; NbExp=5; IntAct=EBI-11037868, EBI-16118096;
CC -!- SUBCELLULAR LOCATION: Melanosome {ECO:0000269|PubMed:17081065}.
CC Note=Identified by mass spectrometry in melanosome fractions from stage
CC I to stage IV. {ECO:0000269|PubMed:17081065}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:25957687}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P26453}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:P18572}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000250|UniProtKB:P18572}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC {ECO:0000269|PubMed:11992541, ECO:0000269|PubMed:15688292,
CC ECO:0000269|PubMed:15946952, ECO:0000269|PubMed:17127621,
CC ECO:0000269|PubMed:21536654, ECO:0000269|PubMed:25825981,
CC ECO:0000269|PubMed:26195724, ECO:0000269|PubMed:28409866,
CC ECO:0000269|PubMed:29739904}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P26453}. Endosome {ECO:0000269|PubMed:29739904}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:15688292}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:P26453}.
CC Basolateral cell membrane {ECO:0000269|PubMed:17267690}; Single-pass
CC type I membrane protein {ECO:0000250|UniProtKB:P26453}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane
CC {ECO:0000269|PubMed:21536654}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P26453}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane
CC {ECO:0000269|PubMed:21536654}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P26453}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Long, Basigin-1 {ECO:0000303|PubMed:25957687};
CC IsoId=P35613-1; Sequence=Displayed;
CC Name=2; Synonyms=Short, Basigin-2 {ECO:0000303|PubMed:25957687};
CC IsoId=P35613-2; Sequence=VSP_011501;
CC Name=3; Synonyms=Basigin-3;
CC IsoId=P35613-3; Sequence=VSP_043225;
CC Name=4; Synonyms=Basigin-4;
CC IsoId=P35613-4; Sequence=VSP_043226, VSP_043227;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Retina-specific (PubMed:25957687).
CC Expressed in retinal cone photoreceptors (at protein level)
CC (PubMed:25957687). {ECO:0000269|PubMed:25957687}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in erythrocytes (at protein
CC level) (PubMed:26195724, PubMed:28409866). Highly expressed in melanoma
CC cell lines (at protein level) (PubMed:11992541). Highly expressed in
CC the heart, kidney, skeletal muscle and testis (PubMed:21536654).
CC {ECO:0000269|PubMed:11992541, ECO:0000269|PubMed:21536654,
CC ECO:0000269|PubMed:26195724, ECO:0000269|PubMed:28409866}.
CC -!- TISSUE SPECIFICITY: [Isoform 3]: Highly expressed in the bone marrow,
CC fetal liver, lung, testis and thymus. {ECO:0000269|PubMed:21536654}.
CC -!- TISSUE SPECIFICITY: [Isoform 4]: Highly expressed in the bone marrow,
CC fetal liver, lung, testis and thymus. {ECO:0000269|PubMed:21536654}.
CC -!- PTM: [Isoform 2]: N-glycosylated. {ECO:0000269|PubMed:21536654}.
CC -!- PTM: [Isoform 3]: N-glycosylated. {ECO:0000269|PubMed:21536654}.
CC -!- PTM: [Isoform 4]: N-glycosylated. {ECO:0000269|PubMed:21536654}.
CC -!- BIOTECHNOLOGY: [Isoform 2]: Potential candidate for the development of
CC parasite blood stage vaccines. In vitro and in vivo, neutralizing
CC antibodies are capable of inhibiting merozoite invasion of host
CC erythrocytes. {ECO:0000269|PubMed:26195724}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage.
CC {ECO:0000269|PubMed:21536654}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative promoter usage.
CC {ECO:0000269|PubMed:21536654}.
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation
CC database;
CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=ok";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/bsg/";
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DR EMBL; X64364; CAA45716.1; -; mRNA.
DR EMBL; D45131; BAA08109.1; -; mRNA.
DR EMBL; L10240; AAA68936.1; -; mRNA.
DR EMBL; M87879; AAA91084.1; -; mRNA.
DR EMBL; L20471; AAB41120.1; -; mRNA.
DR EMBL; AF042854; AAD10704.1; -; Genomic_DNA.
DR EMBL; AF042848; AAD10704.1; JOINED; Genomic_DNA.
DR EMBL; AF042849; AAD10704.1; JOINED; Genomic_DNA.
DR EMBL; AF042850; AAD10704.1; JOINED; Genomic_DNA.
DR EMBL; AF042851; AAD10704.1; JOINED; Genomic_DNA.
DR EMBL; AF042852; AAD10704.1; JOINED; Genomic_DNA.
DR EMBL; AF042853; AAD10704.1; JOINED; Genomic_DNA.
DR EMBL; AB072923; BAB88938.1; -; mRNA.
DR EMBL; AB085790; BAC76828.1; -; mRNA.
DR EMBL; AF548371; AAN40694.1; -; mRNA.
DR EMBL; GU557064; ADD31881.1; -; mRNA.
DR EMBL; GU557065; ADD31882.1; -; mRNA.
DR EMBL; AY358113; AAQ88480.1; -; mRNA.
DR EMBL; AY942196; AAX20110.1; -; Genomic_DNA.
DR EMBL; AC005559; AAC33279.1; -; Genomic_DNA.
DR EMBL; CH471242; EAW61181.1; -; Genomic_DNA.
DR EMBL; CH471242; EAW61185.1; -; Genomic_DNA.
DR EMBL; BC009040; AAH09040.1; -; mRNA.
DR CCDS; CCDS12032.1; -. [P35613-3]
DR CCDS; CCDS12033.1; -. [P35613-1]
DR CCDS; CCDS12034.1; -. [P35613-2]
DR CCDS; CCDS58635.1; -. [P35613-3]
DR PIR; A46506; A46506.
DR RefSeq; NP_001309172.1; NM_001322243.1. [P35613-2]
DR RefSeq; NP_001719.2; NM_001728.3. [P35613-1]
DR RefSeq; NP_940991.1; NM_198589.2. [P35613-2]
DR RefSeq; NP_940992.1; NM_198590.2. [P35613-3]
DR RefSeq; NP_940993.1; NM_198591.2. [P35613-3]
DR RefSeq; XP_016882662.1; XM_017027173.1. [P35613-1]
DR PDB; 3B5H; X-ray; 2.80 A; A/B/C/D=140-321.
DR PDB; 3I84; X-ray; 2.00 A; A/B=13-219.
DR PDB; 3I85; X-ray; 2.50 A; A/B=13-219.
DR PDB; 3QQN; X-ray; 2.31 A; A/B=23-138.
DR PDB; 3QR2; X-ray; 2.30 A; A/B=23-138.
DR PDB; 4U0Q; X-ray; 3.10 A; B/D=1-385.
DR PDB; 5X0T; X-ray; 2.50 A; E/F=138-217.
DR PDB; 5XF0; NMR; -; A=215-321.
DR PDB; 6LYY; EM; 3.60 A; B=140-385.
DR PDB; 6LZ0; EM; 3.60 A; B=140-385.
DR PDB; 7CKO; EM; 2.95 A; B=140-385.
DR PDB; 7CKR; EM; 3.00 A; B=140-385.
DR PDB; 7DA5; EM; 3.30 A; B=140-385.
DR PDB; 7DAA; X-ray; 2.51 A; A=219-385.
DR PDB; 7DCE; EM; 3.80 A; B=219-385.
DR PDBsum; 3B5H; -.
DR PDBsum; 3I84; -.
DR PDBsum; 3I85; -.
DR PDBsum; 3QQN; -.
DR PDBsum; 3QR2; -.
DR PDBsum; 4U0Q; -.
DR PDBsum; 5X0T; -.
DR PDBsum; 5XF0; -.
DR PDBsum; 6LYY; -.
DR PDBsum; 6LZ0; -.
DR PDBsum; 7CKO; -.
DR PDBsum; 7CKR; -.
DR PDBsum; 7DA5; -.
DR PDBsum; 7DAA; -.
DR PDBsum; 7DCE; -.
DR AlphaFoldDB; P35613; -.
DR BMRB; P35613; -.
DR SMR; P35613; -.
DR BioGRID; 107147; 599.
DR CORUM; P35613; -.
DR DIP; DIP-50310N; -.
DR IntAct; P35613; 168.
DR MINT; P35613; -.
DR STRING; 9606.ENSP00000333769; -.
DR ChEMBL; CHEMBL3580492; -.
DR TCDB; 8.A.23.1.1; the basigin (basigin) family.
DR GlyConnect; 1027; 9 N-Linked glycans (2 sites).
DR GlyGen; P35613; 5 sites, 8 N-linked glycans (2 sites), 3 O-linked glycans (2 sites).
DR iPTMnet; P35613; -.
DR MetOSite; P35613; -.
DR PhosphoSitePlus; P35613; -.
DR SwissPalm; P35613; -.
DR BioMuta; BSG; -.
DR DMDM; 51704273; -.
DR CPTAC; CPTAC-319; -.
DR CPTAC; CPTAC-320; -.
DR EPD; P35613; -.
DR jPOST; P35613; -.
DR MassIVE; P35613; -.
DR MaxQB; P35613; -.
DR PaxDb; P35613; -.
DR PeptideAtlas; P35613; -.
DR PRIDE; P35613; -.
DR ProteomicsDB; 55113; -. [P35613-1]
DR ProteomicsDB; 55114; -. [P35613-2]
DR ProteomicsDB; 55115; -. [P35613-3]
DR ProteomicsDB; 55116; -. [P35613-4]
DR TopDownProteomics; P35613-1; -. [P35613-1]
DR TopDownProteomics; P35613-2; -. [P35613-2]
DR TopDownProteomics; P35613-3; -. [P35613-3]
DR ABCD; P35613; 86 sequenced antibodies.
DR Antibodypedia; 3719; 2112 antibodies from 48 providers.
DR DNASU; 682; -.
DR Ensembl; ENST00000333511.9; ENSP00000333769.3; ENSG00000172270.22. [P35613-1]
DR Ensembl; ENST00000346916.9; ENSP00000344707.4; ENSG00000172270.22. [P35613-3]
DR Ensembl; ENST00000353555.9; ENSP00000343809.4; ENSG00000172270.22. [P35613-2]
DR Ensembl; ENST00000545507.6; ENSP00000473664.1; ENSG00000172270.22. [P35613-3]
DR Ensembl; ENST00000573784.6; ENSP00000473393.2; ENSG00000172270.22. [P35613-3]
DR Ensembl; ENST00000576984.3; ENSP00000473528.2; ENSG00000172270.22. [P35613-3]
DR Ensembl; ENST00000680065.1; ENSP00000506020.1; ENSG00000172270.22. [P35613-3]
DR GeneID; 682; -.
DR KEGG; hsa:682; -.
DR MANE-Select; ENST00000333511.9; ENSP00000333769.3; NM_001728.4; NP_001719.2.
DR UCSC; uc002loy.5; human. [P35613-1]
DR CTD; 682; -.
DR DisGeNET; 682; -.
DR GeneCards; BSG; -.
DR HGNC; HGNC:1116; BSG.
DR HPA; ENSG00000172270; Low tissue specificity.
DR MIM; 109480; gene.
DR MIM; 111380; phenotype.
DR neXtProt; NX_P35613; -.
DR OpenTargets; ENSG00000172270; -.
DR PharmGKB; PA25433; -.
DR VEuPathDB; HostDB:ENSG00000172270; -.
DR eggNOG; ENOG502QPKN; Eukaryota.
DR GeneTree; ENSGT00940000159142; -.
DR HOGENOM; CLU_058449_0_0_1; -.
DR InParanoid; P35613; -.
DR OMA; WWFEGND; -.
DR OrthoDB; 1021787at2759; -.
DR PhylomeDB; P35613; -.
DR TreeFam; TF326759; -.
DR PathwayCommons; P35613; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-210991; Basigin interactions.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-433692; Proton-coupled monocarboxylate transport.
DR Reactome; R-HSA-5619070; Defective SLC16A1 causes symptomatic deficiency in lactate transport (SDLT).
DR Reactome; R-HSA-70268; Pyruvate metabolism.
DR Reactome; R-HSA-9749641; Aspirin ADME.
DR SignaLink; P35613; -.
DR BioGRID-ORCS; 682; 66 hits in 1077 CRISPR screens.
DR ChiTaRS; BSG; human.
DR EvolutionaryTrace; P35613; -.
DR GeneWiki; Basigin; -.
DR GenomeRNAi; 682; -.
DR Pharos; P35613; Tbio.
DR PRO; PR:P35613; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P35613; protein.
DR Bgee; ENSG00000172270; Expressed in apex of heart and 191 other tissues.
DR ExpressionAtlas; P35613; baseline and differential.
DR Genevisible; P35613; HS.
DR GO; GO:0002080; C:acrosomal membrane; IEA:Ensembl.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; IDA:UniProtKB.
DR GO; GO:0001618; F:virus receptor activity; IMP:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0061154; P:endothelial tube morphogenesis; IDA:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0003407; P:neural retina development; ISS:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; IMP:UniProtKB.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IDA:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:UniProtKB.
DR GO; GO:1904466; P:positive regulation of matrix metallopeptidase secretion; IDA:UniProtKB.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IDA:UniProtKB.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; IDA:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:ARUK-UCL.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0046689; P:response to mercury ion; IEA:Ensembl.
DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR044157; Basigin.
DR InterPro; IPR043204; Basigin-like.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR PANTHER; PTHR10075; PTHR10075; 1.
DR PANTHER; PTHR10075:SF12; PTHR10075:SF12; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Alternative splicing;
KW Angiogenesis; Blood group antigen; Cell membrane; Cell projection;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; Endosome;
KW Glycoprotein; Host cell receptor for virus entry; Host-virus interaction;
KW Immunoglobulin domain; Lectin; Mannose-binding; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT CHAIN 22..385
FT /note="Basigin"
FT /id="PRO_0000014518"
FT TOPO_DOM 138..323
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P26453"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P26453"
FT DOMAIN 37..120
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 138..219
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 221..315
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 353..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..108
FT /evidence="ECO:0000269|PubMed:21620857,
FT ECO:0007744|PDB:3QQN, ECO:0007744|PDB:3QR2"
FT DISULFID 157..203
FT /evidence="ECO:0000269|PubMed:18430721,
FT ECO:0000269|PubMed:19768682, ECO:0000269|PubMed:25132548,
FT ECO:0000269|Ref.60, ECO:0007744|PDB:3B5H,
FT ECO:0007744|PDB:3I84, ECO:0007744|PDB:4U0Q,
FT ECO:0007744|PDB:5X0T"
FT DISULFID 242..301
FT /evidence="ECO:0000269|PubMed:18430721,
FT ECO:0000269|PubMed:25132548, ECO:0007744|PDB:3B5H,
FT ECO:0007744|PDB:4U0Q"
FT VAR_SEQ 1..209
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:21536654"
FT /id="VSP_043225"
FT VAR_SEQ 1..11
FT /note="MAAALFVLLGF -> MKQSDASPQER (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:21536654"
FT /id="VSP_043226"
FT VAR_SEQ 12..191
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:21536654"
FT /id="VSP_043227"
FT VAR_SEQ 24..139
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:1634773, ECO:0000303|PubMed:7812975"
FT /id="VSP_011501"
FT VARIANT 13
FT /note="L -> V (in dbSNP:rs201850688)"
FT /evidence="ECO:0000269|PubMed:32867305"
FT /id="VAR_084546"
FT VARIANT 16
FT /note="T -> A (in dbSNP:rs11551906)"
FT /evidence="ECO:0000269|PubMed:32867305"
FT /id="VAR_084547"
FT VARIANT 26
FT /note="V -> F (in dbSNP:rs144824657)"
FT /evidence="ECO:0000269|PubMed:32867305"
FT /id="VAR_084548"
FT VARIANT 152
FT /note="K -> N (no effect on the interaction with
FT P.falciparum RH5; dbSNP:rs14704)"
FT /evidence="ECO:0000269|PubMed:22080952"
FT /id="VAR_082637"
FT VARIANT 176
FT /note="V -> L (no effect on the interaction with
FT P.falciparum RH5; dbSNP:rs2229662)"
FT /evidence="ECO:0000269|PubMed:22080952"
FT /id="VAR_082638"
FT VARIANT 206
FT /note="L -> P (loss of interaction with P.falciparum RH5;
FT dbSNP:rs55911144)"
FT /evidence="ECO:0000269|PubMed:22080952"
FT /id="VAR_082639"
FT VARIANT 208
FT /note="E -> K (in Ok(A-); 2-fold reduction in the binding
FT affinity for P.falciparum RH5 with reduced erythrocyte
FT invasion by P.falciparum isolates 3D7 and Dd2;
FT dbSNP:rs104894669)"
FT /evidence="ECO:0000269|PubMed:22080952,
FT ECO:0000269|PubMed:9130641"
FT /id="VAR_013574"
FT VARIANT 269
FT /note="G -> V (loss of interaction with P.falciparum RH5;
FT dbSNP:rs1803203)"
FT /evidence="ECO:0000269|PubMed:22080952"
FT /id="VAR_011720"
FT MUTAGEN 67
FT /note="C->M: Loss of ability to stimulate interleukin-6
FT secretion."
FT /evidence="ECO:0000269|PubMed:21620857"
FT MUTAGEN 160
FT /note="N->D: No effect on the interaction with P.falciparum
FT RH5; when associated with D-268 and D-302."
FT /evidence="ECO:0000269|PubMed:22080952"
FT MUTAGEN 268
FT /note="N->D: No effect on the interaction with P.falciparum
FT RH5; when associated with D-160 and D-302."
FT /evidence="ECO:0000269|PubMed:22080952"
FT MUTAGEN 302
FT /note="N->D: No effect on the interaction with P.falciparum
FT RH5; when associated with D-160 and D-268."
FT /evidence="ECO:0000269|PubMed:22080952"
FT CONFLICT 328
FT /note="F -> L (in Ref. 2; BAC76828)"
FT /evidence="ECO:0000305"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:3QR2"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:3QR2"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:3QR2"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:3QR2"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:3QR2"
FT STRAND 79..95
FT /evidence="ECO:0007829|PDB:3QR2"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3QR2"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:3QR2"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:3QR2"
FT STRAND 128..137
FT /evidence="ECO:0007829|PDB:3QR2"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:3I84"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:3I84"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:3I84"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:3I84"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:3I84"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3I84"
FT STRAND 199..207
FT /evidence="ECO:0007829|PDB:3I84"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:3I84"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:7DAA"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:7DAA"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:7DAA"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:7DAA"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:7DAA"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:3B5H"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:7CKO"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:3B5H"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:7DAA"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:7DAA"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:7DAA"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:7DAA"
FT STRAND 308..318
FT /evidence="ECO:0007829|PDB:7DAA"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:7CKO"
FT HELIX 326..353
FT /evidence="ECO:0007829|PDB:7CKO"
FT REGION P35613-2:195..199
FT /note="Essential for interaction with KDR/VEGFR2"
FT /evidence="ECO:0000269|PubMed:25825981"
FT MUTAGEN P35613-2:27
FT /note="F->L: Severe reduction in the interaction with
FT P.falciparum RH5."
FT /evidence="ECO:0000269|PubMed:24297912"
FT MUTAGEN P35613-2:32
FT /note="D->E: No effect on the interaction with P.falciparum
FT RH5."
FT /evidence="ECO:0000269|PubMed:24297912"
FT MUTAGEN P35613-2:75
FT /note="K->E: No effect on the interaction with P.falciparum
FT RH5."
FT /evidence="ECO:0000269|PubMed:24297912"
FT MUTAGEN P35613-2:100
FT /note="Q->K: Severe reduction in the interaction with
FT P.falciparum RH5."
FT /evidence="ECO:0000269|PubMed:24297912"
FT MUTAGEN P35613-2:102
FT /note="H->HH: Severe reduction in the interaction with
FT P.falciparum RH5."
FT /evidence="ECO:0000269|PubMed:24297912"
FT MUTAGEN P35613-2:144
FT /note="D->A: Reduced interaction with KDR/VEGFR2."
FT /evidence="ECO:0000269|PubMed:25825981"
FT MUTAGEN P35613-2:180..181
FT /note="PG->AA: Loss of its ability to mediate chemotactic
FT activity of PPIA/CYPA."
FT /evidence="ECO:0000269|PubMed:11943775"
FT MUTAGEN P35613-2:182
FT /note="Q->A: Reduced interaction with KDR/VEGFR2.
FT Significant loss of interaction with KDR/VEGFR2; when
FT associated with A-184."
FT /evidence="ECO:0000269|PubMed:25825981"
FT MUTAGEN P35613-2:184
FT /note="R->A: Reduced interaction with KDR/VEGFR2.
FT Significant loss of interaction with KDR/VEGFR2; when
FT associated with A-182."
FT /evidence="ECO:0000269|PubMed:25825981"
FT MUTAGEN P35613-2:195
FT /note="Q->A: Reduced interaction with KDR/VEGFR2. Complete
FT loss of interaction with KDR/VEGFR2 when associated with A-
FT 199."
FT /evidence="ECO:0000269|PubMed:25825981"
FT MUTAGEN P35613-2:199
FT /note="T->A: Reduced interaction with KDR/VEGFR2. Complete
FT loss of interaction with KDR/VEGFR2; when associated with
FT A-195."
FT /evidence="ECO:0000269|PubMed:25825981"
FT MUTAGEN P35613-2:211
FT /note="P->A: Loss of interaction with PPIL2."
FT /evidence="ECO:0000269|PubMed:15946952"
SQ SEQUENCE 385 AA; 42200 MW; D74C37455BF26685 CRC64;
MAAALFVLLG FALLGTHGAS GAAGFVQAPL SQQRWVGGSV ELHCEAVGSP VPEIQWWFEG
QGPNDTCSQL WDGARLDRVH IHATYHQHAA STISIDTLVE EDTGTYECRA SNDPDRNHLT
RAPRVKWVRA QAVVLVLEPG TVFTTVEDLG SKILLTCSLN DSATEVTGHR WLKGGVVLKE
DALPGQKTEF KVDSDDQWGE YSCVFLPEPM GTANIQLHGP PRVKAVKSSE HINEGETAML
VCKSESVPPV TDWAWYKITD SEDKALMNGS ESRFFVSSSQ GRSELHIENL NMEADPGQYR
CNGTSSKGSD QAIITLRVRS HLAALWPFLG IVAEVLVLVT IIFIYEKRRK PEDVLDDDDA
GSAPLKSSGQ HQNDKGKNVR QRNSS
