ID   TMM47_CANLF             Reviewed;         181 AA.
AC   Q9XSV3;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Transmembrane protein 47;
DE   AltName: Full=Brain cell membrane protein 1;
DE   AltName: Full=Transmembrane 4 superfamily member 10;
GN   Name=TMEM47; Synonyms=BCMP1, TM4SF10;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Thyroid;
RX   PubMed=11472633; DOI=10.1186/1471-2164-2-3;
RA   Christophe-Hobertus C., Szpirer C., Guyon R., Christophe D.;
RT   "Identification of the gene encoding brain cell membrane protein 1 (BCMP1),
RT   a putative four-transmembrane protein distantly related to the peripheral
RT   myelin protein 22 / epithelial membrane proteins and the claudins.";
RL   BMC Genomics 2:3-3(2001).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CTNNB1; CTNNA1; PRKCI
RP   AND PARD6B.
RX   PubMed=26990309; DOI=10.1002/dvdy.24404;
RA   Dong Y., Simske J.S.;
RT   "The vertebrate claudin/PMP22/EMP22/MP20 family protein TMEM47 regulates
RT   epithelial cell junction maturation and morphogenesis.";
RL   Dev. Dyn. 245:653-666(2016).
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 (PubMed:26990309). During podocyte differentiation may
CC       negatively regulate activity of FYN and subsequently the abundance of
CC       nephrin (By similarity). {ECO:0000250|UniProtKB:Q9JJG6,
CC       ECO:0000269|PubMed:26990309}.
CC   -!- SUBUNIT: Interacts with CTNNB1, CTNNA1, PRKCI, PARD6B
CC       (PubMed:26990309). Interacts with FYB1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9JJG6, ECO:0000269|PubMed:26990309}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}. Cell junction, adherens junction
CC       {ECO:0000269|PubMed:26990309}. Note=Colocalizes with FYB1 at cell-cell
CC       contacts in podocytes. {ECO:0000250|UniProtKB:Q9JJG6}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain.
CC       {ECO:0000269|PubMed:11472633}.
CC   -!- SIMILARITY: Belongs to the TMEM47 family. {ECO:0000305}.
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DR   EMBL; AJ243320; CAB45864.1; -; mRNA.
DR   RefSeq; NP_001003045.1; NM_001003045.1.
DR   AlphaFoldDB; Q9XSV3; -.
DR   SMR; Q9XSV3; -.
DR   STRING; 9615.ENSCAFP00000020352; -.
DR   PaxDb; Q9XSV3; -.
DR   Ensembl; ENSCAFT00030037933; ENSCAFP00030033094; ENSCAFG00030020668.
DR   Ensembl; ENSCAFT00040027709; ENSCAFP00040024068; ENSCAFG00040015040.
DR   Ensembl; ENSCAFT00845038489; ENSCAFP00845030132; ENSCAFG00845021814.
DR   GeneID; 403572; -.
DR   KEGG; cfa:403572; -.
DR   CTD; 83604; -.
DR   VEuPathDB; HostDB:ENSCAFG00845021814; -.
DR   eggNOG; KOG4671; Eukaryota.
DR   GeneTree; ENSGT00530000063484; -.
DR   HOGENOM; CLU_120054_1_0_1; -.
DR   InParanoid; Q9XSV3; -.
DR   OMA; EWSCNST; -.
DR   OrthoDB; 1307601at2759; -.
DR   TreeFam; TF312855; -.
DR   Proteomes; UP000002254; Chromosome X.
DR   Bgee; ENSCAFG00000013807; Expressed in spinal cord and 45 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   1: Evidence at protein 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_0000072572"
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