TM147_CAPHI
ID TM147_CAPHI Reviewed; 224 AA.
AC I6VSD2;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Transmembrane protein 147;
GN Name=TMEM147;
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION (MICROBIAL INFECTION), SUBCELLULAR
RP LOCATION, INTERACTION WITH H.CONTORTUS GAL-1, AND TISSUE SPECIFICITY.
RX PubMed=27337943; DOI=10.1186/s13071-016-1640-0;
RA Li Y., Yuan C., Wang L., Lu M., Wang Y., Wen Y., Yan R., Xu L., Song X.,
RA Li X.;
RT "Transmembrane protein 147 (TMEM147): another partner protein of Haemonchus
RT contortus galectin on the goat peripheral blood mononuclear cells (PBMC).";
RL Parasit. Vectors 9:355-355(2016).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH H.CONTORTUS GAL-1.
RX PubMed=28870237; DOI=10.1186/s13071-017-2353-8;
RA Lu M., Tian X., Yang X., Yuan C., Ehsan M., Liu X., Yan R., Xu L., Song X.,
RA Li X.;
RT "The N- and C-terminal carbohydrate recognition domains of Haemonchus
RT contortus galectin bind to distinct receptors of goat PBMC and contribute
RT differently to its immunomodulatory functions in host-parasite
RT interactions.";
RL Parasit. Vectors 10:409-409(2017).
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 -!- FUNCTION: (Microbial infection) Involved in the immunomodulatory
CC effects exerted by H.contortus GAL-1 on host peripheral blood
CC mononuclear cells to down-regulate host immune response.
CC {ECO:0000269|PubMed:27337943}.
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 -!- SUBUNIT: (Microbial infection) Interacts with H.contortus GAL-1 (via
CC domain galectin 2). {ECO:0000269|PubMed:27337943}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9BVK8}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:27337943}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in T-cells, B-cells and monocytes.
CC {ECO:0000269|PubMed:27337943}.
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DR EMBL; LWLT01000020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; JQ923484; AFN27531.1; -; mRNA.
DR RefSeq; NP_001301238.1; NM_001314309.1.
DR AlphaFoldDB; I6VSD2; -.
DR SMR; I6VSD2; -.
DR STRING; 9925.ENSCHIP00000026618; -.
DR Ensembl; ENSCHIT00000034483; ENSCHIP00000026618; ENSCHIG00000022872.
DR GeneID; 102181068; -.
DR KEGG; chx:102181068; -.
DR CTD; 10430; -.
DR GeneTree; ENSGT00390000013276; -.
DR OMA; MKSTVDL; -.
DR OrthoDB; 1388283at2759; -.
DR Proteomes; UP000291000; Chromosome 18.
DR Bgee; ENSCHIG00000022872; Expressed in longissimus thoracis muscle and 18 other tissues.
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; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0001817; P:regulation of cytokine production; IMP:UniProtKB.
DR GO; GO:0032944; P:regulation of mononuclear cell proliferation; IMP:UniProtKB.
DR GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0050764; P:regulation of phagocytosis; IMP:UniProtKB.
DR InterPro; IPR019164; TMEM147.
DR PANTHER; PTHR12869; PTHR12869; 1.
DR Pfam; PF09767; DUF2053; 1.
PE 1: Evidence at protein 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_0000448884"
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
