BASI_BOVIN
ID BASI_BOVIN Reviewed; 205 AA.
AC Q865R3;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Basigin;
DE AltName: Full=EMMPRIN;
DE AltName: CD_antigen=CD147;
DE Flags: Precursor; Fragment;
GN Name=BSG;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Endometrium;
RA Sato T., Takita M., Noguchi Y., Konno S., Hirata M., Hashizume K., Ito A.;
RT "Expression of EMMPRIN mRNA in bovine endometrium.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
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, SLC16A12, SLC16A11, ATP1B2, MAG,
CC L1CAM and AJAP1 (By similarity). Interacts with SLC16A3; interaction
CC mediates SLC16A3 targeting to the plasma membrane (By similarity).
CC Interacts with PPIL2; regulates BSG transport to the cell membrane (By
CC similarity). Interacts with XKR8; promoting its localization at the
CC cell membrane (By similarity). {ECO:0000250|UniProtKB:P18572,
CC ECO:0000250|UniProtKB:P26453, 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; AB091679; BAC67167.1; -; mRNA.
DR AlphaFoldDB; Q865R3; -.
DR BMRB; Q865R3; -.
DR SMR; Q865R3; -.
DR PRIDE; Q865R3; -.
DR InParanoid; Q865R3; -.
DR Proteomes; UP000009136; Unplaced.
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; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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: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: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; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 2: Evidence at transcript level;
KW Angiogenesis; Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Immunoglobulin domain; Lectin; Mannose-binding; Membrane;
KW Receptor; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..>205
FT /note="Basigin"
FT /id="PRO_0000014516"
FT TOPO_DOM 19..>205
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P26453"
FT DOMAIN 19..103
FT /note="Ig-like C2-type"
FT DOMAIN 105..199
FT /note="Ig-like V-type"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P35613"
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"
FT NON_TER 205
SQ SEQUENCE 205 AA; 22119 MW; 15215BD36C5A38C0 CRC64;
MAAALFVLLG FALLGTHGAS GAAGTVFTTV EDLGSKILLT CSLNDSATEV TGHRWLKGGV
VLKEDALPGQ KTEFKVDSDD QWGEYSCVFL PEPMGTANIQ LHGPPRVKAV KSSEHINEGE
TAMLVCKSES VPPVTDWAWY KITDSEDKAL MNGSESRFFV SSSQGRSELH IENLNMEADP
GQYRCNGTSS KGSDQAIITL RVRSH
