T184A_RAT
ID T184A_RAT Reviewed; 425 AA.
AC Q4QQS1; Q5XHY9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Transmembrane protein 184A;
GN Name=Tmem184a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
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
CC (PubMed:26769966). May be involved in vesicle transport in exocrine
CC cells and Sertoli cells (By similarity). {ECO:0000250|UniProtKB:Q3UFJ6,
CC ECO:0000269|PubMed:26769966}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26769966};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear
CC region {ECO:0000269|PubMed:26769966}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q3UFJ6}; Multi-pass membrane protein
CC {ECO:0000305}. Endosome {ECO:0000250|UniProtKB:Q3UFJ6}. Cytoplasmic
CC vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q3UFJ6}.
CC Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q1RMW2}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Colocalizes with CAV1
CC (PubMed:26769966). {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH83910.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC083910; AAH83910.1; ALT_INIT; mRNA.
DR EMBL; BC098056; AAH98056.1; -; mRNA.
DR RefSeq; NP_001020584.1; NM_001025413.1.
DR RefSeq; XP_006249001.1; XM_006248939.3.
DR AlphaFoldDB; Q4QQS1; -.
DR STRING; 10116.ENSRNOP00000001718; -.
DR iPTMnet; Q4QQS1; -.
DR PhosphoSitePlus; Q4QQS1; -.
DR PaxDb; Q4QQS1; -.
DR GeneID; 304325; -.
DR KEGG; rno:304325; -.
DR UCSC; RGD:1306702; rat.
DR CTD; 202915; -.
DR RGD; 1306702; Tmem184a.
DR VEuPathDB; HostDB:ENSRNOG00000001275; -.
DR eggNOG; KOG2641; Eukaryota.
DR HOGENOM; CLU_012923_3_0_1; -.
DR InParanoid; Q4QQS1; -.
DR PhylomeDB; Q4QQS1; -.
DR TreeFam; TF314160; -.
DR PRO; PR:Q4QQS1; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001275; Expressed in stomach and 14 other tissues.
DR ExpressionAtlas; Q4QQS1; baseline and differential.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS: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; ISS: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; ISS:UniProtKB.
DR GO; GO:0018992; P:germ-line sex determination; ISO:RGD.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR GO; GO:0051046; P:regulation of secretion; ISO:RGD.
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..425
FT /note="Transmembrane protein 184A"
FT /id="PRO_0000300469"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 375..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 46878 MW; 80EFAF7D81D02C22 CRC64;
MRNASGFLKT AGAPLVSATW LPPSPPPAMP MVAAGPQMER VDNGSQGAPQ LFLTSALARG
VSGVFVWTAL LLTGHQIYSH LRSYTVPREQ RFVIRLLFIV PIYAFDSWLS LLLLGGHPYY
VYFDSVRDCY EAFVIYSFLT LCFQYLGGES AIMAEIRGKP IRSSCFYGTC CLRGMSYSIT
FLRFCKQATL QFCIVKPVMA LITIILQAFD KYHDGDFNIH SGYLYVTLVY NASVSLALYA
LFLFYFATRD LLRPFEPVLK FLTIKAIIFL SFWQGMLLAI LERCGVIPEV QAVDGTRVGA
GTLAAGYQNF LICIEMLFAS LALRYAFPSQ VYSEKKNSPA PPAPMQSISS GLKETISPQD
IVQDAIHNFS PAYQQYTQQS THEAPGPGQG GHPSPSTHPG PASGSGGGKK SRNIEKRMLI
PSEDL
