TM182_CHICK
ID TM182_CHICK Reviewed; 233 AA.
AC A0A1D5NY17;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 2.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Transmembrane protein 182;
DE Flags: Precursor;
GN Name=TMEM182;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP INTERACTION WITH ITGB1.
RX PubMed=34427057; DOI=10.1002/jcsm.12767;
RA Luo W., Lin Z., Chen J., Chen G., Zhang S., Liu M., Li H., He D., Liang S.,
RA Luo Q., Zhang D., Nie Q., Zhang X.;
RT "TMEM182 interacts with integrin beta 1 and regulates myoblast
RT differentiation and muscle regeneration.";
RL J. Cachexia Sarcopenia Muscle 12:1704-1723(2021).
CC -!- FUNCTION: Negatively regulates myogenesis and skeletal muscle
CC regeneration via its association with ITGB1 (PubMed:34427057).
CC Modulates ITGB1 activation by decreasing ITGB1-LAMB1 interaction and
CC inhibiting ITGB1-mediated intracellular signaling during myogenesis
CC (PubMed:34427057). {ECO:0000269|PubMed:34427057}.
CC -!- SUBUNIT: Interacts with ITGB1. {ECO:0000269|PubMed:34427057}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:34427057};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle and adipose tissue.
CC {ECO:0000269|PubMed:34427057}.
CC -!- INDUCTION: Up-regulated during myoblast differentiation.
CC {ECO:0000269|PubMed:34427057}.
CC -!- SIMILARITY: Belongs to the TMEM182 family. {ECO:0000305}.
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DR EMBL; AADN05000806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9031.ENSGALP00000041117; -.
DR Ensembl; ENSGALT00000064494; ENSGALP00000045272; ENSGALG00000038936.
DR VEuPathDB; HostDB:geneid_418721; -.
DR eggNOG; ENOG502QVS4; Eukaryota.
DR GeneTree; ENSGT00390000017581; -.
DR OMA; WLLVTEV; -.
DR OrthoDB; 1246131at2759; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000038936; Expressed in muscle tissue and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0014906; P:myotube cell development involved in skeletal muscle regeneration; IMP:UniProtKB.
DR GO; GO:0014908; P:myotube differentiation involved in skeletal muscle regeneration; IMP:UniProtKB.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; IMP:UniProtKB.
DR GO; GO:1901740; P:negative regulation of myoblast fusion; IMP:UniProtKB.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR InterPro; IPR026763; TMEM182.
DR PANTHER; PTHR32012; PTHR32012; 1.
DR Pfam; PF13903; Claudin_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Myogenesis; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..233
FT /note="Transmembrane protein 182"
FT /evidence="ECO:0000255"
FT /id="PRO_0000454749"
FT TOPO_DOM 27..117
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..203
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 52..62
FT /note="Interaction with ITGB1"
FT /evidence="ECO:0000269|PubMed:34427057"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 233 AA; 26287 MW; 491F3A1DD258D742 CRC64;
MKLSVGIFFG GLFAALGVLL FLVAFGTDYW LLATEIGRCS KAPEDAGTEK ATFHHEGFFW
RCWFSGNVRE HNTSMWKFWY TNQSPSKNCT HAYLSPFPHI RDEHNSTSYD SAVIYRGFWT
VLMLLGVITI VMASFLIICA APFASHILYK AGGGFYILAG VLFSLVVVMY VIWVQAMADL
ENYTNMKKMD CPDFAVYVRY GWSFMLAPIG VFFALLAGML FLLVGRAIYL NSD
