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PARM1_RAT
ID   PARM1_RAT               Reviewed;         296 AA.
AC   Q6P9X9; Q9Z0P0;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Prostate androgen-regulated mucin-like protein 1 homolog;
DE            Short=PARM-1;
DE   AltName: Full=Castration-induced prostatic apoptosis-related protein 1;
DE            Short=CIPAR-1;
DE   AltName: Full=Prostatic androgen-repressed message 1 protein;
DE   Flags: Precursor;
GN   Name=Parm1; Synonyms=Cipar1;
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], FUNCTION, AND INDUCTION.
RC   STRAIN=Wistar;
RX   PubMed=10499539; DOI=10.1210/endo.140.10.7097;
RA   Bruyninx M., Hennuy B., Cornet A., Houssa P., Daukandt M., Reiter E.,
RA   Poncin J., Closset J., Hennen G.;
RT   "A novel gene overexpressed in the prostate of castrated rats: hormonal
RT   regulation, relationship to apoptosis and to acquired prostatic cell
RT   androgen independence.";
RL   Endocrinology 140:4789-4799(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
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   [3]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=Wistar;
RX   PubMed=12772192; DOI=10.1002/pros.10254;
RA   Cornet A.M., Hanon E., Reiter E.R., Bruyninx M., Nguyen V.H., Hennuy B.R.,
RA   Hennen G.P., Closset J.L.;
RT   "Prostatic androgen repressed message-1 (PARM-1) may play a role in
RT   prostatic cell immortalisation.";
RL   Prostate 56:220-230(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION BY
RP   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   -!- FUNCTION: May regulate TLP1 expression and telomerase activity, thus
CC       enabling certain prostatic cells to resist apoptosis.
CC       {ECO:0000269|PubMed:10499539, ECO:0000269|PubMed:12772192}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250};
CC       Single-pass type I membrane protein {ECO:0000250}. Endosome membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in prostate. Detected in other organs at
CC       low levels, these include the heart and various tissues of the
CC       urogenital tract. Not detected in mammary gland.
CC       {ECO:0000269|PubMed:12772192}.
CC   -!- INDUCTION: Induced in prostate, after castration. This induction is
CC       reversed by androgen supplementation. {ECO:0000269|PubMed:10499539}.
CC   -!- PTM: Highly N-glycosylated and O-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PARM family. {ECO:0000305}.
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DR   EMBL; AJ010750; CAB38095.1; -; mRNA.
DR   EMBL; BC060539; AAH60539.1; -; mRNA.
DR   RefSeq; NP_775137.1; NM_173114.1.
DR   AlphaFoldDB; Q6P9X9; -.
DR   STRING; 10116.ENSRNOP00000003472; -.
DR   GlyGen; Q6P9X9; 4 sites.
DR   iPTMnet; Q6P9X9; -.
DR   PhosphoSitePlus; Q6P9X9; -.
DR   PaxDb; Q6P9X9; -.
DR   GeneID; 286894; -.
DR   KEGG; rno:286894; -.
DR   UCSC; RGD:708342; rat.
DR   CTD; 25849; -.
DR   RGD; 708342; Parm1.
DR   eggNOG; ENOG502S50N; Eukaryota.
DR   InParanoid; Q6P9X9; -.
DR   OrthoDB; 1404104at2759; -.
DR   PhylomeDB; Q6P9X9; -.
DR   PRO; PR:Q6P9X9; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; NAS:RGD.
DR   GO; GO:0051973; P:positive regulation of telomerase activity; IMP:UniProtKB.
DR   InterPro; IPR031431; PARM1.
DR   PANTHER; PTHR35453; PTHR35453; 1.
DR   Pfam; PF17061; PARM; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Endosome; Glycoprotein; Golgi apparatus; Membrane;
KW   Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..296
FT                   /note="Prostate androgen-regulated mucin-like protein 1
FT                   homolog"
FT                   /id="PRO_0000045501"
FT   TOPO_DOM        21..244
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        266..296
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          73..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         284
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        17
FT                   /note="R -> M (in Ref. 1; CAB38095)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        284
FT                   /note="S -> SGS (in Ref. 1; CAB38095)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   296 AA;  30729 MW;  450846B6BD760617 CRC64;
     MVCKALITLC IFAAGLRVQG SPTPTLLPVS LTTKSTAPMA TWTTSAQHTA MATTPVASAT
     HNASVLRTTA ASLTSQLPTH PREEAVTSPP LKREVNSTDS SPTGFSSNSS GIHLAPTPEE
     HSLGSPETSV PATGSQSPTL LFSQGPTSAS TSPATSPSEP LSASVTSNHS STVNNIQPTG
     APMAPASPTE EHSSSHTPTS HVTEPVPKEK SPQDTEPGKV ICESETTTPF LIMQEVENAL
     SSGSIAAITV TVIAVVLLVF GAAAYLKIRH SSYGRLLDDH DYGSWGNYNN PLYDDS
 
 
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