BASI_RAT
ID BASI_RAT Reviewed; 388 AA.
AC P26453; Q7TNP1;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Basigin;
DE AltName: Full=Glycoprotein CE9;
DE AltName: Full=OX-47 antigen;
DE AltName: CD_antigen=CD147;
DE Flags: Precursor;
GN Name=Bsg;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY (ISOFORM 2).
RC STRAIN=PVG X DA;
RX PubMed=2009910; DOI=10.1002/eji.1830210320;
RA Fossum S., Mallet S., Barclay A.N.;
RT "The MRC OX-47 antigen is a member of the immunoglobulin superfamily with
RT an unusual transmembrane sequence.";
RL Eur. J. Immunol. 21:671-679(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2),
RP AND TISSUE SPECIFICITY (ISOFORM 2).
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8425897; DOI=10.1083/jcb.120.3.687;
RA Nehme C.L., Cesario M.M., Myles D.G., Koppel D.E., Bartles J.R.;
RT "Breaching the diffusion barrier that compartmentalizes the transmembrane
RT glycoprotein CE9 to the posterior-tail plasma membrane domain of the rat
RT spermatozoon.";
RL J. Cell Biol. 120:687-694(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; 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 [4]
RP PROTEIN SEQUENCE OF 177-222; 228-239; 244-276; 315-320 AND 352-369, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [5]
RP INTERACTION WITH SLC16A1 AND SLC16A3 (ISOFORM 2), FUNCTION (ISOFORM 2), AND
RP SUBCELLULAR LOCATION (ISOFORM 2).
RX PubMed=10921872; DOI=10.1093/emboj/19.15.3896;
RA Kirk P., Wilson M.C., Heddle C., Brown M.H., Barclay A.N., Halestrap A.P.;
RT "CD147 is tightly associated with lactate transporters MCT1 and MCT4 and
RT facilitates their cell surface expression.";
RL EMBO J. 19:3896-3904(2000).
RN [6]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=12141934; DOI=10.1530/rep.0.1240219;
RA Xiao L.J., Diao H.L., Ma X.H., Ding N.Z., Kadomatsu K., Muramatsu T.,
RA Yang Z.M.;
RT "Basigin expression and hormonal regulation in the rat uterus during the
RT peri-implantation period.";
RL Reproduction 124:219-225(2002).
RN [7]
RP INTERACTION WITH SLC16A1 (ISOFORM 2), SUBUNIT (ISOFORM 2), SUBCELLULAR
RP LOCATION (ISOFORM 2), AND TOPOLOGY.
RX PubMed=11719518; DOI=10.1074/jbc.m109658200;
RA Wilson M.C., Meredith D., Halestrap A.P.;
RT "Fluorescence resonance energy transfer studies on the interaction between
RT the lactate transporter MCT1 and CD147 provide information on the topology
RT and stoichiometry of the complex in situ.";
RL J. Biol. Chem. 277:3666-3672(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-357 AND SER-371, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
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 (By similarity). 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 (By similarity).
CC {ECO:0000250|UniProtKB:P18572}.
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 and SLC16A3
CC to the plasma membrane (PubMed:10921872). Acts as a coreceptor for
CC vascular endothelial growth factor receptor 2 (KDR/VEGFR2) in
CC endothelial cells enhancing its VEGFA-mediated activation and
CC downstream signaling (By similarity). Promotes angiogenesis through
CC EPAS1/HIF2A-mediated up-regulation of VEGFA and KDR/VEGFR2 in
CC endothelial cells (By similarity). Plays an important role in
CC spermatogenesis; mediates interactions between germ cells and Sertoli
CC cell and is essential for the development/differentiation of germ cells
CC to round spermatids (By similarity). {ECO:0000250|UniProtKB:P18572,
CC ECO:0000250|UniProtKB:P35613, ECO:0000269|PubMed:10921872}.
CC -!- SUBUNIT: [Isoform 1]: Homooligomer (By similarity). Interacts with
CC NXNL1, SLC2A1 and SLC16A1/GLUT1 (By similarity). Interacts with XKR8;
CC promoting its localization at the cell membrane (By similarity).
CC {ECO:0000250|UniProtKB:P17790, ECO:0000250|UniProtKB:P35613}.
CC -!- SUBUNIT: [Isoform 2]: Homooligomer (Probable). Interacts with
CC SLC16A1/GLUT1 (PubMed:10921872). Interacts with SLC16A3; interaction
CC mediates SLC16A3 targeting to the plasma membrane (PubMed:11719518).
CC Interacts with VEGFA, KDR/VEGFR2, PPIA/CYPA, SLC16A12, SLC16A11,
CC ATP1B2, MAG, L1CAM and AJAP1 (By similarity). Interacts with PPIL2;
CC regulates BSG transport to the cell membrane (By similarity).
CC {ECO:0000250|UniProtKB:P18572, ECO:0000250|UniProtKB:P35613,
CC ECO:0000269|PubMed:10921872, ECO:0000269|PubMed:11719518,
CC ECO:0000305|PubMed:11719518}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000250|UniProtKB:P35613}; Single-pass type I membrane protein
CC {ECO:0000303|PubMed:11719518}. 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:11719518}; Single-pass type I membrane protein
CC {ECO:0000303|PubMed:11719518}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P35613}; Single-pass type I membrane protein
CC {ECO:0000303|PubMed:11719518}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:P35613}; Single-pass type I membrane protein
CC {ECO:0000303|PubMed:11719518}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Basigin-2;
CC IsoId=P26453-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P26453-2; Sequence=VSP_011503;
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in the skeletal muscle,
CC liver, small intestine, kidney, testis, brain, heart and spleen
CC (PubMed:8425897). Also present in various immature cells and endothelia
CC (PubMed:2009910). {ECO:0000269|PubMed:2009910,
CC ECO:0000269|PubMed:8425897}.
CC -!- DEVELOPMENTAL STAGE: In uterus during peri-implantation period strongly
CC expressed in the luminal epithelium on day 1 of pregnancy and gradually
CC decreased to a basal concentration from day 3 to day 5 of pregnancy.
CC Strongly expressed in the implanting blastocyst and primary decidua on
CC day 6 of pregnancy. {ECO:0000269|PubMed:12141934}.
CC -!- INDUCTION: By activation of lymphocytes by mitogens. By estrogen in the
CC uterine epithelium of ovariectomized animals.
CC {ECO:0000269|PubMed:12141934}.
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DR EMBL; X54640; CAA38452.1; -; mRNA.
DR EMBL; X67215; CAA47655.1; -; mRNA.
DR EMBL; AY120888; AAM81604.1; -; mRNA.
DR PIR; S15674; S15674.
DR RefSeq; NP_001103352.1; NM_001109882.1. [P26453-1]
DR RefSeq; NP_036915.1; NM_012783.3. [P26453-2]
DR AlphaFoldDB; P26453; -.
DR SMR; P26453; -.
DR BioGRID; 247286; 1.
DR IntAct; P26453; 1.
DR STRING; 10116.ENSRNOP00000011275; -.
DR GlyGen; P26453; 3 sites, 5 N-linked glycans (1 site).
DR iPTMnet; P26453; -.
DR PhosphoSitePlus; P26453; -.
DR SwissPalm; P26453; -.
DR jPOST; P26453; -.
DR PaxDb; P26453; -.
DR PRIDE; P26453; -.
DR Ensembl; ENSRNOT00000011275; ENSRNOP00000011275; ENSRNOG00000008414. [P26453-1]
DR Ensembl; ENSRNOT00000044275; ENSRNOP00000050252; ENSRNOG00000008414. [P26453-2]
DR GeneID; 25246; -.
DR KEGG; rno:25246; -.
DR UCSC; RGD:2220; rat. [P26453-1]
DR CTD; 682; -.
DR RGD; 2220; Bsg.
DR eggNOG; ENOG502QPKN; Eukaryota.
DR GeneTree; ENSGT00940000159142; -.
DR HOGENOM; CLU_058449_0_0_1; -.
DR InParanoid; P26453; -.
DR OMA; WWFEGND; -.
DR OrthoDB; 1021787at2759; -.
DR PhylomeDB; P26453; -.
DR Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR Reactome; R-RNO-210991; Basigin interactions.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR Reactome; R-RNO-433692; Proton-coupled monocarboxylate transport.
DR Reactome; R-RNO-70268; Pyruvate metabolism.
DR Reactome; R-RNO-9749641; Aspirin ADME.
DR PRO; PR:P26453; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000008414; Expressed in adult mammalian kidney and 19 other tissues.
DR ExpressionAtlas; P26453; baseline and differential.
DR Genevisible; P26453; RN.
DR GO; GO:0002080; C:acrosomal membrane; ISO:RGD.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
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; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
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:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0046697; P:decidualization; IEP:RGD.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007566; P:embryo implantation; IEP:RGD.
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; ISS:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISO:RGD.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEP:RGD.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISS:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR GO; GO:0046689; P:response to mercury ion; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISS: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; Cell membrane; Cell projection; Differentiation;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Immunoglobulin domain; Lectin; Mannose-binding; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Spermatogenesis;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..388
FT /note="Basigin"
FT /id="PRO_0000014521"
FT TOPO_DOM 23..326
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:11719518"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11719518"
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..320
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 355..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 357
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 25..140
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2009910,
FT ECO:0000303|PubMed:8425897"
FT /id="VSP_011503"
SQ SEQUENCE 388 AA; 42436 MW; 3D655169F537E3D4 CRC64;
MAAALLLALA FTFLSGQGAC AAAGFLKAPM SQEQWAGGSV VLHCEAVGSP MPEIQWWFEG
NEPNDSCSQL WDGARLDRVH IHATYRQHAA STLSVDGLAA EDTGTYECRA SSDPDRNHLT
RPPRVKWVRA QASVVVLEPG TIVTSVQEVD SKTQLTCFLN SSGIDIVGHR WMRGGKVLQE
DTLPDLQMKY TVDADDRSGE YSCIFLPEPV GRGNINVEGP PRIKVGKKSE HASEGEFVKL
ICKSEASHPP VDEWVWFKTS DTGDQTISNG TEANSKYVII STPELSELII SDLDMNVDPG
TYVCNATNSQ GSARETISLR VRSRLAALWP FLGIVAEVLV LVTIIFIYEK RRKPDQTLDE
DDPGAAPLKG SGSHLNDKDK NVRQRNAT
