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TM147_BOVIN
ID   TM147_BOVIN             Reviewed;         224 AA.
AC   Q3SZR6;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Transmembrane protein 147;
GN   Name=TMEM147;
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=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of a ribosome-associated endoplasmic reticulum (ER)
CC       translocon complex involved in multi-pass membrane protein transport
CC       into the ER membrane and biogenesis. Together with SEC61 and TMCO1,
CC       forms the lipid-filled cavity at the center of the translocon where
CC       TMEM147 may insert hydrophobic segments of mutli-pass membrane proteins
CC       from the lumen into de central membrane cavity in a process gated by
CC       SEC61, and TMCO1 may insert hydrophobic segments of nascent chains from
CC       the cytosol into the cavity. Acts as a negative regulator of CHRM3
CC       function, most likely by interfering with its trafficking to the cell
CC       membrane. Negatively regulates CHRM3-mediated calcium mobilization and
CC       activation of RPS6KA1/p90RSK activity. {ECO:0000250|UniProtKB:Q9BVK8}.
CC   -!- SUBUNIT: Forms a complex with NCLN/Nicalin and NOMO, resulting in a
CC       stabilization of the 3 proteins, which are otherwise quickly degraded
CC       by the proteasome. Interacts with CHRM3, CHRM1 and AVPR2. The ribosome-
CC       associated ER translocon complex includes SEC61A1, SEC61B, SEC61G,
CC       TMCO1, CCDC47, NCLN/Nicalin, NOMO and TMEM147; in the absence of
CC       ribosomes, only the complex forms with NCLN/Nicalin, NOMO and TMEM147
CC       remains intact. {ECO:0000250|UniProtKB:Q9BVK8}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9BVK8}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:I6VSD2}; Multi-pass
CC       membrane protein {ECO:0000255}.
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DR   EMBL; BC102737; AAI02738.1; -; mRNA.
DR   RefSeq; NP_001029796.1; NM_001034624.1.
DR   AlphaFoldDB; Q3SZR6; -.
DR   SMR; Q3SZR6; -.
DR   STRING; 9913.ENSBTAP00000021170; -.
DR   PaxDb; Q3SZR6; -.
DR   PRIDE; Q3SZR6; -.
DR   Ensembl; ENSBTAT00000021170; ENSBTAP00000021170; ENSBTAG00000015920.
DR   GeneID; 535038; -.
DR   KEGG; bta:535038; -.
DR   CTD; 10430; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015920; -.
DR   VGNC; VGNC:35978; TMEM147.
DR   eggNOG; KOG3236; Eukaryota.
DR   GeneTree; ENSGT00390000013276; -.
DR   HOGENOM; CLU_086813_0_0_1; -.
DR   InParanoid; Q3SZR6; -.
DR   OMA; MKSTVDL; -.
DR   OrthoDB; 1388283at2759; -.
DR   TreeFam; TF314086; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000015920; Expressed in retina and 108 other tissues.
DR   ExpressionAtlas; Q3SZR6; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR   InterPro; IPR019164; TMEM147.
DR   PANTHER; PTHR12869; PTHR12869; 1.
DR   Pfam; PF09767; DUF2053; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Endoplasmic reticulum; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..224
FT                   /note="Transmembrane protein 147"
FT                   /id="PRO_0000271700"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   224 AA;  25321 MW;  90122F2DC80E96D1 CRC64;
     MTLFHFGNCF ALAYFPYFIT YKCSGLSEYN AFWKCVQAGV TYLFVQLCKM LFLATFFPTW
     EGGIYDFIGE FMKASVDVAD LIGLNLVMSR NAGKGEYKIM VAALGWATAE LIMSRCIPLW
     VGARGIEFDW KYIQMSIDSN ISLVHYIVAS AQVWMITRYD LYHTYRPAVL LLMFLSVYKA
     FVMETFVHLC SLGSWTALLA RALVTGLLAL STLALYVAVV NVHS
 
 
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