BASI_CRIGR
ID BASI_CRIGR Reviewed; 249 AA.
AC Q99PA3;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Basigin;
DE AltName: CD_antigen=CD147;
DE Flags: Fragment;
GN Name=BSG;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=11353871; DOI=10.1073/pnas.111583198;
RA Pushkarsky T., Zybarth G., Dubrovsky L., Yurchenko V., Tang H., Guo H.,
RA Toole B., Sherry B., Bukrinsky M.;
RT "CD147 facilitates HIV-1 infection by interacting with virus-associated
RT cyclophilin A.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6360-6365(2001).
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. Interacts with
CC PPIL2; regulates BSG transport to the cell membrane (By similarity).
CC Interacts with XKR8; promoting its localization at the cell membrane
CC (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; AF320819; AAK09323.1; -; mRNA.
DR AlphaFoldDB; Q99PA3; -.
DR SMR; Q99PA3; -.
DR STRING; 10029.XP_007615025.1; -.
DR eggNOG; ENOG502QPKN; Eukaryota.
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 InterPro; IPR003598; Ig_sub2.
DR PANTHER; PTHR10075; PTHR10075; 1.
DR PANTHER; PTHR10075:SF12; PTHR10075:SF12; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 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 Phosphoprotein; Receptor; Transmembrane; Transmembrane helix.
FT CHAIN <1..249
FT /note="Basigin"
FT /id="PRO_0000014517"
FT TOPO_DOM <1..187
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P26453"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P26453"
FT DOMAIN 1..82
FT /note="Ig-like C2-type"
FT DOMAIN 84..179
FT /note="Ig-like V-type"
FT REGION 216..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 218
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18572"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35613"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P35613"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P35613"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 20..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 105..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 1
SQ SEQUENCE 249 AA; 27414 MW; A92CDA0154A4C0CE CRC64;
AAGTIQTSVN DVGSKTHLTC SLNSSGVDII GHRWMRGGKI LQEDTLPDLQ TQYTVDIDDR
SGDYACIFLP EPVGRSNIVV EGPPRIKVGK KSEHSSEGEN VRLICKSESS HPPVTEWSWF
KTSDSGDQLI TNSSESKYVV ISTADRSELT ISNLDINSDP GTYMCNATNT QGSVQEIMTL
RVRSRLAALW PFLGIVAEVL VLVTIIFIYE KRRKPDQTLD EDDPGAAPLK GSGHHMNDKD
KNVRQRNAT
