BASI_MOUSE
ID BASI_MOUSE Reviewed; 389 AA.
AC P18572; Q6LDB0; Q7TSC0;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Basigin;
DE AltName: Full=Basic immunoglobulin superfamily;
DE AltName: Full=HT7 antigen;
DE AltName: Full=Membrane glycoprotein gp42;
DE AltName: CD_antigen=CD147;
DE Flags: Precursor;
GN Name=Bsg;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY (ISOFORM 2).
RC STRAIN=129/Sv;
RX PubMed=2361961; DOI=10.1093/oxfordjournals.jbchem.a123045;
RA Miyauchi T., Kanekura T., Yamaoka A., Ozawa M., Miyazawa S., Muramatsu T.;
RT "Basigin, a new, broadly distributed member of the immunoglobulin
RT superfamily, has strong homology with both the immunoglobulin V domain and
RT the beta-chain of major histocompatibility complex class II antigen.";
RL J. Biochem. 107:316-323(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RC TISSUE=Fibroblast;
RX PubMed=2697642; DOI=10.1016/0378-1119(89)90438-1;
RA Altruda F., Cervella P., Gaeta M.L., Daniele A., Giancotti F., Tarone G.,
RA Stefanuto G., Silengo L.;
RT "Cloning of cDNA for a novel mouse membrane glycoprotein (gp42): shared
RT identity to histocompatibility antigens, immunoglobulins and neural-cell
RT adhesion molecules.";
RL Gene 85:445-452(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=8333335; DOI=10.1007/978-1-4615-2920-0_33;
RA Unger C.M., Seulberger H., Breier G., Albrecht U., Achen M.G., Risau W.;
RT "Expression of the HT7 gene in blood-brain barrier.";
RL Adv. Exp. Med. Biol. 331:211-215(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8576084; DOI=10.1093/oxfordjournals.jbchem.a124971;
RA Miyauchi T., Jimma F., Igakura T., Yu S., Ozawa M., Muramatsu T.;
RT "Structure of the mouse basigin gene, a unique member of the immunoglobulin
RT superfamily.";
RL J. Biochem. 118:717-724(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RX PubMed=2032306; DOI=10.1247/csf.16.23;
RA Kanekura T., Miyauchi T., Tahior M., Muramatsu T.;
RT "Basigin, a new member of the immunoglobulin superfamily: genes in
RT different mammalian species, glycosylation changes in the molecule from
RT adult organs and possible variation in the N-terminal sequences.";
RL Cell Struct. Funct. 16:23-30(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1), AND TISSUE SPECIFICITY (ISOFORMS 1 AND 2).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 [9]
RP PROTEIN SEQUENCE OF N-TERMINUS, PROTEIN SEQUENCE OF 278-286, INTERACTION
RP WITH ATP1B2; MAG AND L1CAM (ISOFORM 2), AND GLYCOSYLATION (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12558975; DOI=10.1046/j.1471-4159.2003.01537.x;
RA Heller M., von der Ohe M., Kleene R., Mohajeri M.H., Schachner M.;
RT "The immunoglobulin-superfamily molecule basigin is a binding protein for
RT oligomannosidic carbohydrates: an anti-idiotypic approach.";
RL J. Neurochem. 84:557-565(2003).
RN [10]
RP PROTEIN SEQUENCE OF 278-286, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [11]
RP FUNCTION (ISOFORM 1), AND DISRUPTION PHENOTYPE.
RX PubMed=10967074;
RA Hori K., Katayama N., Kachi S., Kondo M., Kadomatsu K., Usukura J.,
RA Muramatsu T., Mori S., Miyake Y.;
RT "Retinal dysfunction in basigin deficiency.";
RL Invest. Ophthalmol. Vis. Sci. 41:3128-3133(2000).
RN [12]
RP FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1), DISRUPTION
RP PHENOTYPE, AND TISSUE SPECIFICITY (ISOFORM 1).
RX PubMed=11273674; DOI=10.1006/exer.2000.0974;
RA Ochrietor J.D., Moroz T.M., Kadomatsu K., Muramatsu T., Linser P.J.;
RT "Retinal degeneration following failed photoreceptor maturation in
RT 5A11/basigin null mice.";
RL Exp. Eye Res. 72:467-477(2001).
RN [13]
RP FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1), DISRUPTION
RP PHENOTYPE, AND TISSUE SPECIFICITY (ISOFORM 1).
RX PubMed=11853760; DOI=10.1016/s0042-6989(01)00236-x;
RA Ochrietor J.D., Moroz T.P., Clamp M.F., Timmers A.M., Muramatsu T.,
RA Linser P.J.;
RT "Inactivation of the Basigin gene impairs normal retinal development and
RT maturation.";
RL Vision Res. 42:447-453(2002).
RN [14]
RP FUNCTION (ISOFORM 2), AND SUBCELLULAR LOCATION (ISOFORM 2).
RX PubMed=12601063; DOI=10.1167/iovs.02-0552;
RA Philp N.J., Ochrietor J.D., Rudoy C., Muramatsu T., Linser P.J.;
RT "Loss of MCT1, MCT3, and MCT4 expression in the retinal pigment epithelium
RT and neural retina of the 5A11/basigin-null mouse.";
RL Invest. Ophthalmol. Vis. Sci. 44:1305-1311(2003).
RN [15]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=12211060; DOI=10.1002/mrd.10128;
RA Xiao L.J., Chang H., Ding N.Z., Ni H., Kadomatsu K., Yang Z.M.;
RT "Basigin expression and hormonal regulation in mouse uterus during the
RT peri-implantation period.";
RL Mol. Reprod. Dev. 63:47-54(2002).
RN [16]
RP FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), TISSUE SPECIFICITY
RP (IOSFORM 2), AND DEGLYCOSYLATION.
RX PubMed=11882021; DOI=10.1530/rep.0.1230435;
RA Saxena D.K., Oh-Oka T., Kadomatsu K., Muramatsu T., Toshimori K.;
RT "Behaviour of a sperm surface transmembrane glycoprotein basigin during
RT epididymal maturation and its role in fertilization in mice.";
RL Reproduction 123:435-444(2002).
RN [17]
RP DEVELOPMENTAL STAGE.
RX PubMed=15037112; DOI=10.1016/j.exer.2003.12.004;
RA Clamp M.F., Ochrietor J.D., Moroz T.P., Linser P.J.;
RT "Developmental analyses of 5A11/Basigin, 5A11/Basigin-2 and their putative
RT binding partner MCT1 in the mouse eye.";
RL Exp. Eye Res. 78:777-789(2004).
RN [18]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=15095333; DOI=10.1002/mrd.20060;
RA Chang H., Ni H., Ma X.-H., Xu L.-B., Kadomatsu K., Muramatsu T.,
RA Yang Z.-M.;
RT "Basigin expression and regulation in mouse ovary during the sexual
RT maturation and development of corpus luteum.";
RL Mol. Reprod. Dev. 68:135-141(2004).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-358 AND SER-372, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [20]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160 AND ASN-270.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [21]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160; ASN-270 AND ASN-306.
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 [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [23]
RP INTERACTION WITH SLC16A1 AND SLC16A7 (ISOFORM 2), TISSUE SPECIFICITY, AND
RP FUNCTION (ISOFORM 2).
RX PubMed=21792931; DOI=10.1002/jcp.22949;
RA Mannowetz N., Wandernoth P., Wennemuth G.;
RT "Basigin interacts with both MCT1 and MCT2 in murine spermatozoa.";
RL J. Cell. Physiol. 227:2154-2162(2012).
RN [24]
RP FUNCTION (ISOFORM 2), DISRUPTION PHENOTYPE, TISSUE SPECIFICITY (ISOFORM 2),
RP AND GLYCOSYLATION (ISOFORM 2).
RX PubMed=23727514; DOI=10.1016/j.ydbio.2013.05.023;
RA Bi J., Li Y., Sun F., Saalbach A., Klein C., Miller D.J., Hess R.,
RA Nowak R.A.;
RT "Basigin null mutant male mice are sterile and exhibit impaired
RT interactions between germ cells and Sertoli cells.";
RL Dev. Biol. 380:145-156(2013).
RN [25]
RP FUNCTION (ISOFORM 1), INTERACTION WITH NXNL1 (ISOFORM 1), SUBCELLULAR
RP LOCATION (ISOFORM 1), TISSUE SPECIFICITY (ISOFORMS 1 AND 2), AND
RP GLYCOSYLATION (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 [26]
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).
CC -!- FUNCTION: [Isoform 1]: Essential for normal retinal maturation and
CC development (PubMed:10967074, PubMed:11273674, PubMed:11853760). Acts
CC as a retinal cell surface receptor for NXNL1 and plays an important
CC role in NXNL1-mediated survival of retinal cone photoreceptors
CC (PubMed:25957687). In association with glucose transporter
CC SLC16A1/GLUT1 and NXNL1, promotes retinal cone survival by enhancing
CC aerobic glycolysis and accelerating the entry of glucose into
CC photoreceptors (PubMed:25957687). {ECO:0000269|PubMed:10967074,
CC ECO:0000269|PubMed:11273674, ECO:0000269|PubMed:11853760,
CC ECO:0000269|PubMed:25957687}.
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 (By similarity). Plays an important role
CC in targeting the monocarboxylate transporters SLC16A1/GLUT1, SLC16A3
CC and SLC16A8 to the plasma membrane (PubMed:12601063). 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 (By similarity). Promotes
CC angiogenesis through EPAS1/HIF2A-mediated up-regulation of VEGFA and
CC KDR/VEGFR2 in endothelial cells (By similarity). Plays an important
CC role in spermatogenesis; mediates interactions between germ cells and
CC Sertoli cell and is essential for the development/differentiation of
CC germ cells to round spermatids (PubMed:23727514, PubMed:11882021).
CC {ECO:0000250|UniProtKB:P35613, ECO:0000269|PubMed:11882021,
CC ECO:0000269|PubMed:12601063, ECO:0000269|PubMed:23727514}.
CC -!- SUBUNIT: [Isoform 1]: Interacts with NXNL1 (PubMed:25957687). Interacts
CC with SLC2A1 and SLC16A1/GLUT1 (By similarity). Interacts with XKR8;
CC promoting its localization at the cell membrane (PubMed:27503893).
CC {ECO:0000250|UniProtKB:P17790, ECO:0000269|PubMed:25957687,
CC ECO:0000269|PubMed:27503893}.
CC -!- SUBUNIT: [Isoform 2]: Interacts with ATP1B2, MAG and L1CAM
CC (PubMed:12558975). Interacts with SLC16A1/GLUT1 and SLC16A7
CC (PubMed:21792931). Interacts with VEGFA, KDR/VEGFR2, PPIA/CYPA, SLC1A3,
CC SLC16A11 and SLC16A12 (By similarity). Interacts with PPIL2; regulates
CC BSG transport to the cell membrane (By similarity). Interacts with
CC SLC16A3; interaction mediates SLC16A3 targeting to the plasma membrane
CC (By similarity). {ECO:0000250|UniProtKB:P26453,
CC ECO:0000250|UniProtKB:P35613, ECO:0000269|PubMed:12558975,
CC ECO:0000269|PubMed:21792931}.
CC -!- INTERACTION:
CC P18572; Q8BIL5: Hook1; NbExp=2; IntAct=EBI-772883, EBI-4285715;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:11273674, ECO:0000269|PubMed:25957687}; Single-pass
CC type I membrane protein {ECO:0000250|UniProtKB:P26453}. Photoreceptor
CC inner segment {ECO:0000269|PubMed:11853760,
CC ECO:0000269|PubMed:25957687}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000269|PubMed:25957687}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC {ECO:0000269|PubMed:12601063}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P26453}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P35613}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P26453}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:P35613}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P26453}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=5A11/Basigin {ECO:0000303|PubMed:11273674,
CC ECO:0000303|PubMed:11853760}, Basigin-1 {ECO:0000303|PubMed:25957687};
CC IsoId=P18572-1; Sequence=Displayed;
CC Name=2; Synonyms=5A11/Basigin-2 {ECO:0000303|PubMed:12601063},
CC Basigin-2 {ECO:0000303|PubMed:25957687};
CC IsoId=P18572-2; Sequence=VSP_011502;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Retina-specific (PubMed:12939332,
CC PubMed:11273674, PubMed:11853760, PubMed:25957687). Expressed in both
CC rods and cones (at protein level) (PubMed:25957687).
CC {ECO:0000269|PubMed:11273674, ECO:0000269|PubMed:11853760,
CC ECO:0000269|PubMed:12939332, ECO:0000269|PubMed:25957687}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Testis and caput, corpus and cauda
CC epididymides (at protein level) (PubMed:11882021, PubMed:23727514,
CC PubMed:21792931). Expressed in the brain, lung, liver, kidney, heart,
CC spleen, uterus, retina and skeletal muscle (PubMed:2361961,
CC PubMed:12939332, PubMed:12601063). {ECO:0000269|PubMed:11882021,
CC ECO:0000269|PubMed:12601063, ECO:0000269|PubMed:12939332,
CC ECO:0000269|PubMed:21792931, ECO:0000269|PubMed:2361961,
CC ECO:0000269|PubMed:23727514}.
CC -!- DEVELOPMENTAL STAGE: In developing eye expressed at embryonic days 12
CC dpc, 15 dpc and 18 dpc, and at postnatal days P1, P7, P14, and P21.
CC Expression progressed from a more generalized distribution throughout
CC the undifferentiated neural retina to specific staining of retina-
CC pigmented epithilia, the MCs, photoreceptor cells and the ciliary
CC apparatus. Expression is highest at P21. Isoform 1 and isoform 2 are
CC expressed at equivalent levels at P7, isoform 1 is more abundant at
CC P14, P21 and P28. In uterus during the peri-implantation period
CC strongly expressed in luminal and glandular epithelium on day 1 of
CC pregnancy and gradually decreased to a basal level from day 2-4 of
CC pregnancy. Expression in the sub-luminal stroma was first detected on
CC day 3 of pregnancy and increased on day 4 of pregnancy. On day 5 of
CC pregnancy, the expression of basigin protein and mRNA was only detected
CC in the implanting embryos, and the luminal epithelium and sub-luminal
CC stroma surrounding the embryos. In ovary during sexual maturation
CC expressed in the granulosa cells of preantral follicles at days 20 and
CC 25 after birth. Expressed during corpus luteum formation.
CC {ECO:0000269|PubMed:12211060, ECO:0000269|PubMed:15037112,
CC ECO:0000269|PubMed:15095333}.
CC -!- INDUCTION: By estrogen in the uterine epithelium of ovariectomized
CC animals. By eCG in ovary. {ECO:0000269|PubMed:12211060,
CC ECO:0000269|PubMed:15095333}.
CC -!- PTM: [Isoform 1]: N-glycosylated. {ECO:0000269|PubMed:19349973,
CC ECO:0000269|PubMed:19656770, ECO:0000269|PubMed:25957687}.
CC -!- PTM: [Isoform 2]: N-glycosylated (PubMed:12558975, PubMed:23727514).
CC During spermatogenesis, probably deglycosylated during epididymal
CC transit (PubMed:11882021). {ECO:0000269|PubMed:11882021,
CC ECO:0000269|PubMed:12558975, ECO:0000269|PubMed:23727514}.
CC -!- DISRUPTION PHENOTYPE: Male mice are sterile, testis lack elongated
CC spermatids and mature spermatozoa, spermatogenesis is arrested at the
CC early round spermatid stages before any spermatid differentiation
CC occurrs and a large increase in the number of germ cells undergoing
CC apoptosis is seen in the testis (PubMed:23727514). Mice are visually
CC impaired at the time of eye opening (2 weeks of age), despite normal
CC retina architecture at that age (PubMed:10967074, PubMed:11273674,
CC PubMed:11853760). At visual maturity (3 weeks of age), the
CC photoreceptor outer segments appear less dense and shorter than those
CC of control animals, and at 8 weeks, retinal degeneration is observed
CC (PubMed:10967074, PubMed:11273674, PubMed:11853760).
CC {ECO:0000269|PubMed:10967074, ECO:0000269|PubMed:11273674,
CC ECO:0000269|PubMed:11853760, ECO:0000269|PubMed:23727514}.
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DR EMBL; D00611; BAA00486.1; -; mRNA.
DR EMBL; D82019; BAA11508.1; -; Genomic_DNA.
DR EMBL; S63813; AAB27567.2; -; mRNA.
DR EMBL; Y16256; CAA76140.1; -; mRNA.
DR EMBL; AY089967; AAM09957.1; -; mRNA.
DR EMBL; AK002332; BAB22018.1; -; mRNA.
DR EMBL; BC010270; AAH10270.1; -; mRNA.
DR CCDS; CCDS23985.1; -. [P18572-1]
DR CCDS; CCDS35967.1; -. [P18572-2]
DR PIR; JX0107; JX0107.
DR PIR; S43512; S43512.
DR RefSeq; NP_001070652.1; NM_001077184.1. [P18572-2]
DR RefSeq; NP_033898.1; NM_009768.2. [P18572-1]
DR AlphaFoldDB; P18572; -.
DR SMR; P18572; -.
DR BioGRID; 198392; 10.
DR IntAct; P18572; 2.
DR MINT; P18572; -.
DR STRING; 10090.ENSMUSP00000070751; -.
DR GlyConnect; 2147; 7 N-Linked glycans (2 sites).
DR GlyGen; P18572; 3 sites, 7 N-linked glycans (2 sites).
DR iPTMnet; P18572; -.
DR PhosphoSitePlus; P18572; -.
DR SwissPalm; P18572; -.
DR EPD; P18572; -.
DR jPOST; P18572; -.
DR MaxQB; P18572; -.
DR PaxDb; P18572; -.
DR PeptideAtlas; P18572; -.
DR PRIDE; P18572; -.
DR ProteomicsDB; 273438; -. [P18572-1]
DR ProteomicsDB; 273439; -. [P18572-2]
DR ABCD; P18572; 22 sequenced antibodies.
DR Antibodypedia; 3719; 2112 antibodies from 48 providers.
DR DNASU; 12215; -.
DR Ensembl; ENSMUST00000067036; ENSMUSP00000070751; ENSMUSG00000023175. [P18572-1]
DR Ensembl; ENSMUST00000179781; ENSMUSP00000136487; ENSMUSG00000023175. [P18572-2]
DR GeneID; 12215; -.
DR KEGG; mmu:12215; -.
DR UCSC; uc007fzl.1; mouse. [P18572-1]
DR UCSC; uc007fzm.1; mouse. [P18572-2]
DR CTD; 682; -.
DR MGI; MGI:88208; Bsg.
DR VEuPathDB; HostDB:ENSMUSG00000023175; -.
DR eggNOG; ENOG502QPKN; Eukaryota.
DR GeneTree; ENSGT00940000159142; -.
DR HOGENOM; CLU_058449_0_0_1; -.
DR InParanoid; P18572; -.
DR OMA; WWFEGND; -.
DR OrthoDB; 1021787at2759; -.
DR PhylomeDB; P18572; -.
DR TreeFam; TF326759; -.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-210991; Basigin interactions.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-433692; Proton-coupled monocarboxylate transport.
DR Reactome; R-MMU-70268; Pyruvate metabolism.
DR Reactome; R-MMU-9749641; Aspirin ADME.
DR BioGRID-ORCS; 12215; 11 hits in 70 CRISPR screens.
DR ChiTaRS; Bsg; mouse.
DR PRO; PR:P18572; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P18572; protein.
DR Bgee; ENSMUSG00000023175; Expressed in placenta labyrinth and 334 other tissues.
DR ExpressionAtlas; P18572; baseline and differential.
DR Genevisible; P18572; MM.
DR GO; GO:0002080; C:acrosomal membrane; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0001618; F:virus receptor activity; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
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; ISS: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; IMP:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISO:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:1904466; P:positive regulation of matrix metallopeptidase secretion; ISO:MGI.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISS:UniProtKB.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
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 GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
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 Alternative splicing; Angiogenesis; Cell membrane; Cell projection;
KW Differentiation; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Immunoglobulin domain; Lectin;
KW Mannose-binding; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Signal; Spermatogenesis; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT CHAIN 22..389
FT /note="Basigin"
FT /id="PRO_0000014519"
FT TOPO_DOM 22..325
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P26453"
FT TRANSMEM 326..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..389
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..319
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 356..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 358
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 44..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 157..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 242..305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 24..139
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:2361961,
FT ECO:0000303|PubMed:8333335"
FT /id="VSP_011502"
SQ SEQUENCE 389 AA; 42445 MW; B1E484C3386BEB20 CRC64;
MAAALLLALA FTLLSGQGAC AAAGFLKAPL SQERWAGGSV VLHCEAVGSP IPEIQWWFEG
NAPNDSCSQL WDGARLDRVH IHAAYRQHAA SSLSVDGLTA EDTGTYECRA SSDPDRNHLT
RPPRVKWVRA QASVVVLEPG TIQTSVQEVN SKTQLTCSLN SSGVDIVGHR WMRGGKVLQE
DTLPDLHTKY IVDADDRSGE YSCIFLPEPV GRSEINVEGP PRIKVGKKSE HSSEGELAKL
VCKSDASYPP ITDWFWFKTS DTGEEEAITN STEANGKYVV VSTPEKSQLT ISNLDVNVDP
GTYVCNATNA QGTTRETISL RVRSRMAALW PFLGIVAEVL VLVTIIFIYE KRRKPDQTLD
EDDPGAAPLK GSGTHMNDKD KNVRQRNAT
