ID   TMM47_BOVIN             Reviewed;         181 AA.
AC   Q1JPA3;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Transmembrane protein 47;
DE   AltName: Full=Transmembrane 4 superfamily member 10;
GN   Name=TMEM47; Synonyms=TM4SF10;
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].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulates cell junction organization in epithelial cells. May
CC       play a role in the transition from adherens junction to tight junction
CC       assembly. May regulate F-actin polymerization required for tight
CC       junctional localization dynamics and affect the junctional localization
CC       of PARD6B. During podocyte differentiation may negatively regulate
CC       activity of FYN and subsequently the abundance of nephrin (By
CC       similarity). {ECO:0000250|UniProtKB:Q9JJG6,
CC       ECO:0000250|UniProtKB:Q9XSV3}.
CC   -!- SUBUNIT: Interacts with CTNNB1, CTNNA1, PRKCI, PARD6B, FYB1.
CC       {ECO:0000250|UniProtKB:Q9JJG6, ECO:0000250|UniProtKB:Q9XSV3}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}. Cell junction, adherens junction
CC       {ECO:0000250|UniProtKB:Q9XSV3}. Note=Colocalizes with FYB1 at cell-cell
CC       contacts in podocytes. {ECO:0000250|UniProtKB:Q9JJG6}.
CC   -!- SIMILARITY: Belongs to the TMEM47 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BT025450; ABF57406.1; -; mRNA.
DR   EMBL; BC142425; AAI42426.1; -; mRNA.
DR   EMBL; BC151822; AAI51823.1; -; mRNA.
DR   RefSeq; NP_001069730.1; NM_001076262.1.
DR   AlphaFoldDB; Q1JPA3; -.
DR   SMR; Q1JPA3; -.
DR   STRING; 9913.ENSBTAP00000019004; -.
DR   PaxDb; Q1JPA3; -.
DR   Ensembl; ENSBTAT00000019004; ENSBTAP00000019004; ENSBTAG00000014304.
DR   GeneID; 541164; -.
DR   KEGG; bta:541164; -.
DR   CTD; 83604; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014304; -.
DR   VGNC; VGNC:36090; TMEM47.
DR   eggNOG; KOG4671; Eukaryota.
DR   GeneTree; ENSGT00530000063484; -.
DR   HOGENOM; CLU_120054_1_0_1; -.
DR   InParanoid; Q1JPA3; -.
DR   OMA; EWSCNST; -.
DR   OrthoDB; 1307601at2759; -.
DR   TreeFam; TF312855; -.
DR   Proteomes; UP000009136; Chromosome X.
DR   Bgee; ENSBTAG00000014304; Expressed in occipital lobe and 106 other tissues.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   InterPro; IPR015664; P53_induced.
DR   PANTHER; PTHR14399; PTHR14399; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell junction; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQJ4"
FT   CHAIN           2..181
FT                   /note="Transmembrane protein 47"
FT                   /id="PRO_0000344625"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQJ4"
SQ   SEQUENCE   181 AA;  19998 MW;  A73A03FD0C3B3FBB CRC64;
     MASAGSGMEE VRVSVLTPLK LVGLVCIFLA LCLDLGAVLS PAWVTADHQY YLSLWESCRK
     PASLDIWHCE STLSSDWQIA TLALLLGGAA IILIAFLVGL ISICVGSRRR FYRPVAVMLF
     AAVVLQVCSL VLYPIKFIET VSLKIYHEFN WGYGLAWGAT IFSFGGAILY CLNPKNYEDY
     Y