BASI_CHICK
ID BASI_CHICK Reviewed; 388 AA.
AC P17790; Q6X975;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Basigin;
DE AltName: Full=5A11 antigen;
DE AltName: Full=Blood-brain barrier HT7 antigen;
DE AltName: Full=Neurothelin;
DE Flags: Precursor;
GN Name=BSG;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE,
RP SUBCELLULAR LOCATION (ISOFORM 2), TISSUE SPECIFICITY (ISOFORM 2), AND
RP GLYCOSYLATION (ISOFORM 2).
RX PubMed=2357963; DOI=10.1002/j.1460-2075.1990.tb07384.x;
RA Seulberger H., Lottspeich F., Risau W.;
RT "The inducible blood-brain barrier specific molecule HT7 is a novel
RT immunoglobulin-like cell surface glycoprotein.";
RL EMBO J. 9:2151-2158(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (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 [3]
RP PARTIAL PROTEIN SEQUENCE.
RC STRAIN=White leghorn; TISSUE=Retina;
RX PubMed=8575462;
RA Schlosshauer B., Bauch H., Frank R.;
RT "Neurothelin: amino acid sequence, cell surface dynamics and actin
RT colocalization.";
RL Eur. J. Cell Biol. 68:159-166(1995).
RN [4]
RP FUNCTION (ISOFORM 1), INTERACTION WITH NXNL1; SLC2A1 AND SLC16A1 (ISOFORM
RP 1), SUBCELLULAR LOCATION (ISOFORM 1), AND TISSUE SPECIFICITY (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).
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).
CC {ECO:0000250|UniProtKB:P18572, 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 SLC16A8, SLC16A11 and SLC16A12 to the plasma membrane (By similarity).
CC Acts as a 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).
CC {ECO:0000250|UniProtKB:P35613}.
CC -!- SUBUNIT: [Isoform 1]: Interacts with NXNL1, SLC2A1 and SLC16A1/GLUT1.
CC {ECO:0000269|PubMed:25957687}.
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:2357963}; 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=Long, Basigin-1 {ECO:0000303|PubMed:25957687};
CC IsoId=P17790-1; Sequence=Displayed;
CC Name=2; Synonyms=Short, Basigin-2 {ECO:0000303|PubMed:25957687};
CC IsoId=P17790-2; Sequence=VSP_011504;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Retinal cone photoreceptors (at
CC protein level). {ECO:0000269|PubMed:25957687}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Brain endothelial cells, kidney
CC epithelial cells and erythroblasts (at protein level).
CC {ECO:0000269|PubMed:2357963}.
CC -!- PTM: [Isoform 2]: N-glycosylated. {ECO:0000269|PubMed:2357963}.
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DR EMBL; X52751; CAA36962.1; -; mRNA.
DR EMBL; AY248696; AAP80139.1; -; mRNA.
DR RefSeq; NP_001185919.1; NM_001198990.2. [P17790-1]
DR RefSeq; NP_001185921.1; NM_001198992.1. [P17790-2]
DR AlphaFoldDB; P17790; -.
DR SMR; P17790; -.
DR BioGRID; 691081; 1.
DR STRING; 9031.ENSGALP00000002020; -.
DR MEROPS; I43.951; -.
DR PRIDE; P17790; -.
DR Ensembl; ENSGALT00000002022; ENSGALP00000002020; ENSGALG00000001328. [P17790-1]
DR Ensembl; ENSGALT00000068947; ENSGALP00000054098; ENSGALG00000001328. [P17790-2]
DR GeneID; 770363; -.
DR KEGG; gga:770363; -.
DR CTD; 682; -.
DR VEuPathDB; HostDB:geneid_770363; -.
DR eggNOG; ENOG502QPKN; Eukaryota.
DR GeneTree; ENSGT00940000159142; -.
DR HOGENOM; CLU_058449_0_0_1; -.
DR InParanoid; P17790; -.
DR OMA; WWFEGND; -.
DR OrthoDB; 1021787at2759; -.
DR PhylomeDB; P17790; -.
DR Reactome; R-GGA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-GGA-210991; Basigin interactions.
DR Reactome; R-GGA-373920; Pyruvate metabolism.
DR Reactome; R-GGA-433692; Proton-coupled monocarboxylate transport.
DR Reactome; R-GGA-70268; Pyruvate metabolism.
DR Reactome; R-GGA-9749641; Aspirin ADME.
DR PRO; PR:P17790; -.
DR Proteomes; UP000000539; Chromosome 28.
DR Bgee; ENSGALG00000001328; Expressed in heart and 14 other tissues.
DR ExpressionAtlas; P17790; baseline and differential.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
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; 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:0010575; P:positive regulation of vascular endothelial growth factor production; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; 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; 3.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Angiogenesis; Cell membrane; Cell projection;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Immunoglobulin domain; Membrane; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..388
FT /note="Basigin"
FT /id="PRO_0000014522"
FT TOPO_DOM 27..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..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P26453"
FT DOMAIN 43..131
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 143..218
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 229..323
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 358..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 162..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 250..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 28..144
FT /note="AGFIKSPLSQRRLTQDSVELHCEAVGSPIPEIQWWFEGNEPNETSAQLWDGA
FT WQDRVQINATYNLHSTSTIYIANLTSDDSGTYECRASNDPDRNHLSKSPKVKWIRSQAN
FT VLVIER -> G (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_011504"
SQ SEQUENCE 388 AA; 42414 MW; 9B04428F1A7DE759 CRC64;
MAAGADVPCA VLALLVLGSL AAGGDATAGF IKSPLSQRRL TQDSVELHCE AVGSPIPEIQ
WWFEGNEPNE TSAQLWDGAW QDRVQINATY NLHSTSTIYI ANLTSDDSGT YECRASNDPD
RNHLSKSPKV KWIRSQANVL VIERPVITGQ YSSSADKVVL SCNISAPPTL IKGHKWMLGD
KVLKTDESDA SSYISYTIEG KVEDHSGVYE CIYNTNPVAK GNVSIEVEPQ VVAYKKSEHG
NEGDVGVLTC KSPSYPPVDH WAWYKSGQTV PLESSAGIYN ISRTGNKTEL RILKLNIEQD
MGDYSCNGTN MKGSGSATVN LRVRSRLAAL WPFLGIVAEV LVLVTIIFIY EKRRKPDEVL
DDDDGGSAPL KSNATNHKDK NVRQRNAN
