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MYADM_RAT
ID   MYADM_RAT               Reviewed;         318 AA.
AC   Q6VBQ5;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Myeloid-associated differentiation marker;
DE   AltName: Full=Myeloid up-regulated protein;
GN   Name=Myadm;
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 [MRNA].
RC   STRAIN=Sprague-Dawley;
RA   Zhou G., Dang Y., Jiang L.;
RT   "Cloning of myeloid-associated differentiation marker.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the MAL family. {ECO:0000305}.
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DR   EMBL; AY344060; AAQ22727.1; -; mRNA.
DR   RefSeq; NP_899161.1; NM_183332.1.
DR   AlphaFoldDB; Q6VBQ5; -.
DR   BioGRID; 266784; 3.
DR   IntAct; Q6VBQ5; 2.
DR   MINT; Q6VBQ5; -.
DR   STRING; 10116.ENSRNOP00000022264; -.
DR   iPTMnet; Q6VBQ5; -.
DR   PhosphoSitePlus; Q6VBQ5; -.
DR   jPOST; Q6VBQ5; -.
DR   PaxDb; Q6VBQ5; -.
DR   PRIDE; Q6VBQ5; -.
DR   GeneID; 369016; -.
DR   KEGG; rno:369016; -.
DR   UCSC; RGD:727835; rat.
DR   CTD; 91663; -.
DR   RGD; 727835; Myadm.
DR   eggNOG; KOG4788; Eukaryota.
DR   InParanoid; Q6VBQ5; -.
DR   OrthoDB; 1056604at2759; -.
DR   PhylomeDB; Q6VBQ5; -.
DR   PRO; PR:Q6VBQ5; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045121; C:membrane raft; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0001726; C:ruffle; ISO:RGD.
DR   GO; GO:0061028; P:establishment of endothelial barrier; ISO:RGD.
DR   GO; GO:0031579; P:membrane raft organization; ISO:RGD.
DR   GO; GO:0030837; P:negative regulation of actin filament polymerization; ISO:RGD.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR   GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; ISO:RGD.
DR   GO; GO:0090038; P:negative regulation of protein kinase C signaling; ISO:RGD.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR   GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:RGD.
DR   GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR   InterPro; IPR008253; Marvel.
DR   Pfam; PF01284; MARVEL; 2.
DR   PROSITE; PS51225; MARVEL; 2.
PE   1: Evidence at protein level;
KW   Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..318
FT                   /note="Myeloid-associated differentiation marker"
FT                   /id="PRO_0000232596"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          25..157
FT                   /note="MARVEL 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT   DOMAIN          162..315
FT                   /note="MARVEL 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
SQ   SEQUENCE   318 AA;  35148 MW;  1FBE25CF36BC2B60 CRC64;
     MPVTVTRTTI TTTSSSSTTV GSARALTQPL GLLRLLQLVS TCVAFSLVAS VGAWTGPMGN
     WAMFTWCFCF AVTLIILIEE LGGFQARFPL SWRNFPITFA CYAALFCLSS SIIYPTTYVQ
     FLPHGRSRDH AIAATTFSCV ACLAYATEVA WTRARPGEIT GYMATVPGLL KVFETFVACI
     IFAFISEPSL YQQRPALEWC VAVYAICFIL AAVTVLLNLG DCTNMLPIPF PTFLSGLALL
     SVLLYATAIV LWPLYQFDQR YNSQPRRSMD PSCSRSYVQP NEVCNWDRRL AVSILTGINL
     LAYVSDLVYS TRLVFVKV
 
 
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