TM9S4_BOVIN
ID TM9S4_BOVIN Reviewed; 642 AA.
AC A5D7E2;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Transmembrane 9 superfamily member 4;
DE Flags: Precursor;
GN Name=TM9SF4;
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] OF 1-286.
RC TISSUE=Thymus;
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RT "Bovine genome sequencing program: full-length cDNA sequencing.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-642.
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Associates with proteins harboring glycine-rich transmembrane
CC domains and ensures their efficient localization to the cell surface.
CC {ECO:0000250|UniProtKB:Q92544}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}. Golgi apparatus {ECO:0000250|UniProtKB:Q92544}.
CC Early endosome {ECO:0000250|UniProtKB:Q92544}.
CC -!- SIMILARITY: Belongs to the nonaspanin (TM9SF) (TC 9.A.2) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI40524.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; EH147528; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC140523; AAI40524.1; ALT_INIT; mRNA.
DR RefSeq; NP_001091546.2; NM_001098077.2.
DR AlphaFoldDB; A5D7E2; -.
DR STRING; 9913.ENSBTAP00000001344; -.
DR PaxDb; A5D7E2; -.
DR PRIDE; A5D7E2; -.
DR Ensembl; ENSBTAT00000001344; ENSBTAP00000001344; ENSBTAG00000001015.
DR GeneID; 533562; -.
DR KEGG; bta:533562; -.
DR CTD; 9777; -.
DR VEuPathDB; HostDB:ENSBTAG00000001015; -.
DR VGNC; VGNC:35913; TM9SF4.
DR eggNOG; KOG1278; Eukaryota.
DR GeneTree; ENSGT00940000157198; -.
DR HOGENOM; CLU_010714_4_1_1; -.
DR InParanoid; A5D7E2; -.
DR OMA; CYPKNGT; -.
DR OrthoDB; 641127at2759; -.
DR TreeFam; TF354239; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000001015; Expressed in ascending colon and 105 other tissues.
DR ExpressionAtlas; A5D7E2; baseline and differential.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:Ensembl.
DR GO; GO:0006909; P:phagocytosis; IEA:Ensembl.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:0072657; P:protein localization to membrane; IBA:GO_Central.
DR GO; GO:0051453; P:regulation of intracellular pH; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IEA:Ensembl.
DR InterPro; IPR004240; EMP70.
DR PANTHER; PTHR10766; PTHR10766; 1.
DR Pfam; PF02990; EMP70; 1.
PE 2: Evidence at transcript level;
KW Endosome; Golgi apparatus; Membrane; Phosphoprotein; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..642
FT /note="Transmembrane 9 superfamily member 4"
FT /id="PRO_0000311809"
FT TOPO_DOM 24..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..376
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..449
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..501
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 523..535
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..556
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 557..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..591
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 592..598
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 620..642
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 312
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q92544"
FT CONFLICT 271
FT /note="L -> F (in Ref. 1; EH147528)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 642 AA; 74367 MW; C274C3FF9061EECE CRC64;
MAAAMDWLPW SLLLFSLMCD TGAFYVPGVA PINFHQNDPV EIKAVKLTSS RTQLPYEYYS
LPFCQPSKIT YKAENLGEVL RGDRIVNTPF QVLMNSEKKC EVLCGQSNKP VTLTVEQSRL
VAERISEDYY VHLIADNLPV ATRLELYSNR DGDDKKKEKD VQFEHGYRLG FTDVNKIYLH
NHLSFILYYH REDLEEDREH TYRVVRFEVI PQSVRLEDLK ADEKSSCTLP EGTNSSPQEI
DPTKENQLYF TYSVHWEESD IKWASRWDTY LTMSDVQIHW FSIINSVVVV FFLSGILSMI
IIRTLRKDIA NYNKEDDIED TMEESGWKLV HGDVFRPPQY PMILSSLLGS GIQLFCMILI
VIFVAMLGML SPSSRGALMT TACFLFMFMG VFGGFSAGRL YRTLKGHRWK KGAFCTATLY
PGVVFGICFV LNCFIWGKHS SGAVPFPTMV ALLCMWFGIS LPLVYLGYYF GFRKQPYDNP
VRTNQIPRQI PEQRWYMNRF VGILMAGILP FGAMFIELFF IFSAIWENQF YYLFGFLFLV
FIILVVSCSQ ISIVMVYFQL CAEDYRWWWR NFLVSGGSAF YVLVYAIFYF VNKLDIVEFI
PSLLYFGYTA LMVLSFWLLT GTIGFYAAYM FVRKIYAAVK ID
