TSN12_BOVIN
ID TSN12_BOVIN Reviewed; 305 AA.
AC Q29RH7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Tetraspanin-12;
DE Short=Tspan-12;
GN Name=TSPAN12;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulator of cell surface receptor signal transduction. Plays
CC a central role in retinal vascularization by regulating norrin (NDP)
CC signal transduction. Acts in concert with norrin (NDP) to promote FZD4
CC multimerization and subsequent activation of FZD4, leading to promote
CC accumulation of beta-catenin (CTNNB1) and stimulate LEF/TCF-mediated
CC transcriptional programs. Suprisingly, it only activate the norrin
CC (NDP)-dependent activation of FZD4, while it does not activate the Wnt-
CC dependent activation of FZD4, suggesting the existence of a Wnt-
CC independent signaling that also promote accumulation the beta-catenin
CC (CTNNB1). Acts as a regulator of membrane proteinases such as ADAM10
CC and MMP14/MT1-MMP. Activates ADAM10-dependent cleavage activity of
CC amyloid precursor protein (APP). Activates MMP14/MT1-MMP-dependent
CC cleavage activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of a complex, at least composed of TSPAN12, FZD4 and
CC norrin (NDP) (By similarity). Interacts (when palmitoylated) with
CC ADAM10. Interacts with MMP14/MT1-MMP (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: Palmitoylated; required for interaction with ADAM10. The precise
CC position of palmitoylated residues is unclear and occurs either on Cys-
CC 9, Cys-12 and/or Cys-83 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR EMBL; BC114167; AAI14168.1; -; mRNA.
DR RefSeq; NP_001039977.1; NM_001046512.2.
DR RefSeq; XP_005205711.1; XM_005205654.2.
DR RefSeq; XP_005205712.1; XM_005205655.3.
DR RefSeq; XP_015325742.1; XM_015470256.1.
DR AlphaFoldDB; Q29RH7; -.
DR STRING; 9913.ENSBTAP00000020385; -.
DR PaxDb; Q29RH7; -.
DR GeneID; 613639; -.
DR KEGG; bta:613639; -.
DR CTD; 23554; -.
DR eggNOG; KOG3882; Eukaryota.
DR HOGENOM; CLU_055524_1_0_1; -.
DR InParanoid; Q29RH7; -.
DR OrthoDB; 954168at2759; -.
DR TreeFam; TF316345; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045765; P:regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:1900746; P:regulation of vascular endothelial growth factor signaling pathway; IBA:GO_Central.
DR GO; GO:0010842; P:retina layer formation; ISS:UniProtKB.
DR Gene3D; 1.10.1450.10; -; 1.
DR InterPro; IPR018499; Tetraspanin/Peripherin.
DR InterPro; IPR000301; Tetraspanin_animals.
DR InterPro; IPR018503; Tetraspanin_CS.
DR InterPro; IPR008952; Tetraspanin_EC2_sf.
DR PANTHER; PTHR19282; PTHR19282; 1.
DR Pfam; PF00335; Tetraspanin; 1.
DR PIRSF; PIRSF002419; Tetraspanin; 1.
DR SUPFAM; SSF48652; SSF48652; 1.
DR PROSITE; PS00421; TM4_1; 1.
PE 2: Evidence at transcript level;
KW Angiogenesis; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..305
FT /note="Tetraspanin-12"
FT /id="PRO_0000284964"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..59
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 9
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 12
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 83
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 305 AA; 35418 MW; 4A5DDAAC53B6DF4A CRC64;
MAREDSVKCL RCLLYALNLL FWLMSISVLA VSAWMRDYLN NVLTLTAETR VEEAVILTYF
PVVHPVMIAV CCFLIIVGML GYCGTVKRNL LLLAWYFGSL LVIFCVELAC GVWTYEQEIM
VPVQWSDMVT LKARMTNYGL PRYRWLTHAW NFFQREFKCC GVVYFTDWLE MTEMDWPPDS
CCVREFPGCS KQAHQEDLSD LYQEGCGKKM YSFLRGTKQL QVLRFLGISI GVTQILAMIL
TITLLWALYY DRREPGTDQM MALKNDTTQH LPCHSVELLK PSLSRIFEHT SMANSFNTHF
EMEEL
