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T184A_BOVIN
ID   T184A_BOVIN             Reviewed;         414 AA.
AC   Q1RMW2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Transmembrane protein 184A;
GN   Name=TMEM184A;
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=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=26769966; DOI=10.1074/jbc.m115.681122;
RA   Pugh R.J., Slee J.B., Farwell S.L., Li Y., Barthol T., Patton W.A.,
RA   Lowe-Krentz L.J.;
RT   "Transmembrane protein 184A is a receptor required for vascular smooth
RT   muscle cell responses to heparin.";
RL   J. Biol. Chem. 291:5326-5341(2016).
CC   -!- FUNCTION: Acts as a heparin receptor in vascular cells (By similarity).
CC       May be involved in vesicle transport in exocrine cells and Sertoli
CC       cells (By similarity). {ECO:0000250|UniProtKB:Q3UFJ6,
CC       ECO:0000250|UniProtKB:Q4QQS1}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26769966};
CC       Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear
CC       region {ECO:0000269|PubMed:26769966}. Cytoplasmic vesicle membrane
CC       {ECO:0000269|PubMed:26769966}; Multi-pass membrane protein
CC       {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q3UFJ6};
CC       Multi-pass membrane protein {ECO:0000255}. Endosome
CC       {ECO:0000250|UniProtKB:Q3UFJ6}. Cytoplasmic vesicle, secretory vesicle
CC       membrane {ECO:0000250|UniProtKB:Q3UFJ6}. Note=Colocalizes with CAV1.
CC       {ECO:0000269|PubMed:26769966}.
CC   -!- TISSUE SPECIFICITY: Expressed in vascular cells (at protein level).
CC       {ECO:0000269|PubMed:26769966}.
CC   -!- SIMILARITY: Belongs to the TMEM184 family. {ECO:0000305}.
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DR   EMBL; BC114674; AAI14675.1; -; mRNA.
DR   RefSeq; NP_001039737.1; NM_001046272.1.
DR   RefSeq; XP_010817863.1; XM_010819561.2.
DR   AlphaFoldDB; Q1RMW2; -.
DR   STRING; 9913.ENSBTAP00000006135; -.
DR   PaxDb; Q1RMW2; -.
DR   Ensembl; ENSBTAT00000006135; ENSBTAP00000006135; ENSBTAG00000004676.
DR   Ensembl; ENSBTAT00000070260; ENSBTAP00000070248; ENSBTAG00000004676.
DR   GeneID; 524484; -.
DR   KEGG; bta:524484; -.
DR   CTD; 202915; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004676; -.
DR   VGNC; VGNC:36009; TMEM184A.
DR   eggNOG; KOG2641; Eukaryota.
DR   GeneTree; ENSGT00940000153861; -.
DR   HOGENOM; CLU_012923_3_0_1; -.
DR   InParanoid; Q1RMW2; -.
DR   OMA; CEQRYII; -.
DR   OrthoDB; 462913at2759; -.
DR   TreeFam; TF314160; -.
DR   Proteomes; UP000009136; Chromosome 25.
DR   Bgee; ENSBTAG00000004676; Expressed in surface of tongue and 85 other tissues.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0030667; C:secretory granule membrane; ISS:UniProtKB.
DR   GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR   InterPro; IPR005178; Ostalpha/TMEM184C.
DR   PANTHER; PTHR23423; PTHR23423; 1.
DR   Pfam; PF03619; Solute_trans_a; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Cytoplasmic vesicle; Endosome; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..414
FT                   /note="Transmembrane protein 184A"
FT                   /id="PRO_0000300467"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          364..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..386
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..414
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   414 AA;  45604 MW;  40444949ED7A1664 CRC64;
     MTDTPGLLGT PLAWTPPARP AGPQMERAGN GSQGPGPLFL TSPLARGVSG VFVWAALVLT
     GHQIYLHLRS YTVPHEQRYI IRLLFIVPVY AFDSWLSLLL LGGHQHYIYF DSVRDCYEAF
     VIYSFLSLCF QYLGGESAIM AEIRGKPVRT SCFHGTCCLR GMTYSIGFLR FCKQATLQFC
     IVKPIMALVT IVLQAFGKYH DGDFNVRSGY LYITLVYNAS VSLALYALFL FYSATRELLQ
     PFEPVLKFLT IKAVIFLSFW QGLLLAILER CGVIPEVQVI DGSTVGAGTV AAGYQNFIIC
     IEMLFASIAL RYAFTCQVYS EKTESSPAPS APMQSISSGL KETMSPQDIV QDAIHNFSPA
     YQKYTQQATQ EAPRPGQGSV PSPRTPTHSP DGGPGGGRKG RNVEKRMLIP AEEL
 
 
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