TSN12_CHICK
ID TSN12_CHICK Reviewed; 305 AA.
AC Q5ZIF5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Tetraspanin-12;
DE Short=Tspan-12;
GN Name=TSPAN12; ORFNames=RCJMB04_27b23;
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 [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of a complex, at least composed of TSPAN12, FZD4 and
CC norrin (NDP). {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; AJ720829; CAG32488.1; -; mRNA.
DR RefSeq; NP_001007850.1; NM_001007849.1.
DR RefSeq; XP_015136498.1; XM_015281012.1.
DR RefSeq; XP_015136504.1; XM_015281018.1.
DR AlphaFoldDB; Q5ZIF5; -.
DR STRING; 9031.ENSGALP00000014674; -.
DR PaxDb; Q5ZIF5; -.
DR Ensembl; ENSGALT00000014690; ENSGALP00000014674; ENSGALG00000009029.
DR GeneID; 417763; -.
DR KEGG; gga:417763; -.
DR CTD; 23554; -.
DR VEuPathDB; HostDB:geneid_417763; -.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00510000047764; -.
DR HOGENOM; CLU_055524_1_0_1; -.
DR InParanoid; Q5ZIF5; -.
DR OMA; GCSRSNK; -.
DR OrthoDB; 954168at2759; -.
DR PhylomeDB; Q5ZIF5; -.
DR TreeFam; TF316345; -.
DR PRO; PR:Q5ZIF5; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000009029; Expressed in liver and 14 other tissues.
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_0000294075"
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; 35256 MW; 16CA0BBF725BCC14 CRC64;
MAREDSVRCL RCLLYALNLL FWLMSISVLG VSAWIRDYLN NVLTLTAETR VEEAVILTYF
PVVHPVMIAV CCFLILVGML GYCGTVKRNL LLLVWYFGSL LVIFCVELAC GVWTYEQEIT
VPVQWSDMIT LKARMTNYGL PRYQWLTHAW NFFQREFKCC GVVYFTDWLE MTEMDWPPDS
CCVREFPGCS KQAHHEDLSD LYQEGCGKKM YTFLRGTKQL QVLRFLGISI GVTQILAMIL
TITLLWALYY DRRDPGADQI MSLKNDTSQQ LSCHSVELLK PSLTGIFEHT SMANSFNTHF
EMEEL
