BASI_RABIT
ID BASI_RABIT Reviewed; 270 AA.
AC Q28740;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Basigin;
DE AltName: CD_antigen=CD147;
DE Flags: Precursor;
GN Name=BSG;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=8603097; DOI=10.1016/0167-4889(95)00186-7;
RA Schuster V.L., Lu R., Kanai N., Bao Y., Rosenberg S., Prie D., Ronco P.,
RA Jennings M.L.;
RT "Cloning of the rabbit homologue of mouse 'basigin' and rat 'OX-47': kidney
RT cell type-specific expression, and regulation in collecting duct cells.";
RL Biochim. Biophys. Acta 1311:13-19(1996).
CC -!- FUNCTION: Signaling receptor for cyclophilins, essential for PPIA/CYPA
CC and PPIB/CYPB-dependent signaling related to chemotaxis and adhesion of
CC immune cells (By similarity). Plays an important role in targeting the
CC monocarboxylate transporters SLC16A1/GLUT1, SLC16A3, SLC16A8, SLC16A11
CC and SLC16A12 to the plasma membrane (By similarity). 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).
CC {ECO:0000250|UniProtKB:P35613}.
CC -!- SUBUNIT: Homooligomer (By similarity). Interacts with VEGFA,
CC KDR/VEGFR2, PPIA/CYPA, SLC16A1/GLUT1, SLC1A3, SLC16A12, SLC16A11,
CC ATP1B2, MAG, L1CAM and AJAP1 (By similarity). Interacts with PPIL2;
CC regulates BSG transport to the cell membrane (By similarity). Interacts
CC with XKR8; promoting its localization at the cell membrane (By
CC similarity).Interacts with SLC16A3; interaction mediates SLC16A3
CC targeting to the plasma membrane (By similarity).
CC {ECO:0000250|UniProtKB:P18572, ECO:0000250|UniProtKB:P26453,
CC ECO:0000250|UniProtKB:P35613}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35613};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P26453}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35613}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:P26453}.
CC Basolateral cell membrane {ECO:0000250|UniProtKB:P35613}; Single-pass
CC type I membrane protein {ECO:0000250|UniProtKB:P26453}.
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DR EMBL; U62398; AAB04759.1; -; mRNA.
DR PIR; S65739; S65739.
DR RefSeq; NP_001075843.1; NM_001082374.1.
DR AlphaFoldDB; Q28740; -.
DR SMR; Q28740; -.
DR PRIDE; Q28740; -.
DR GeneID; 100009229; -.
DR KEGG; ocu:100009229; -.
DR CTD; 682; -.
DR InParanoid; Q28740; -.
DR Proteomes; UP000001811; Unplaced.
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; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
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; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0061154; P:endothelial tube morphogenesis; 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; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
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 PANTHER; PTHR10075; PTHR10075; 1.
DR PANTHER; PTHR10075:SF12; PTHR10075:SF12; 1.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Angiogenesis; Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Immunoglobulin domain; Lectin; Mannose-binding; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..270
FT /note="Basigin"
FT /id="PRO_0000014520"
FT TOPO_DOM 22..207
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P26453"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P26453"
FT DOMAIN 22..103
FT /note="Ig-like C2-type"
FT DOMAIN 105..203
FT /note="Ig-like V-type"
FT REGION 239..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35613"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P35613"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P35613"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 126..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 270 AA; 29078 MW; 1CB0737A7B5DA6D1 CRC64;
MAAVLFALLA LALLRAGGAS AAAGTVTTSV QSGDSWVQLT CTLNTSAAGV TGHRWLKGKE
VVKEDQLQGL HTEHNVTGDD RFGKYSCLFL PKDTGEATLT VDGPPRIKAV KKSEHANEGD
SVTLLCKSES FPFVTAWVWY KVADSGDQVI QNGSQSRFFI SHSEAQSELH IKDLDLTSDP
GEYACNGTSL QGTDAAVVTL RVRSRLAALW PFLGIVAEVL VLVTVIFIYE KRRKPDEVLD
DEDAGAAPLK SSGHHVNDDK GKNVRQRNAS
