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PRIC1_RAT
ID   PRIC1_RAT               Reviewed;         831 AA.
AC   Q71QF9;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Prickle-like protein 1;
DE   AltName: Full=REST/NRSF-interacting LIM domain protein 1;
DE   Flags: Precursor;
GN   Name=Prickle1; Synonyms=Rilp;
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] OF 1-135.
RG   Program for rat gene discovery and mapping;
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 86-831.
RC   TISSUE=Brain;
RX   PubMed=14645515; DOI=10.1128/mcb.23.24.9025-9031.2003;
RA   Shimojo M., Hersh L.B.;
RT   "REST/NRSF-interacting LIM domain protein, a putative nuclear translocation
RT   receptor.";
RL   Mol. Cell. Biol. 23:9025-9031(2003).
CC   -!- FUNCTION: Involved in the planar cell polarity pathway that controls
CC       convergent extension during gastrulation and neural tube closure (By
CC       similarity). Convergent extension is a complex morphogenetic process
CC       during which cells elongate, move mediolaterally, and intercalate
CC       between neighboring cells, leading to convergence toward the
CC       mediolateral axis and extension along the anteroposterior axis.
CC       Necessary for nuclear localization of REST. May serve as nuclear
CC       receptor (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with REST. {ECO:0000250|UniProtKB:Q96MT3}.
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}. Cytoplasm,
CC       cytosol {ECO:0000250}. Note=A smaller amount is detected in the
CC       cytosol. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ03034.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AW434734; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AF399843; AAQ03034.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q71QF9; -.
DR   SMR; Q71QF9; -.
DR   IntAct; Q71QF9; 1.
DR   STRING; 10116.ENSRNOP00000031476; -.
DR   iPTMnet; Q71QF9; -.
DR   PhosphoSitePlus; Q71QF9; -.
DR   PaxDb; Q71QF9; -.
DR   PRIDE; Q71QF9; -.
DR   RGD; 735090; Prickle1.
DR   eggNOG; KOG1704; Eukaryota.
DR   InParanoid; Q71QF9; -.
DR   PhylomeDB; Q71QF9; -.
DR   Reactome; R-RNO-4608870; Asymmetric localization of PCP proteins.
DR   PRO; PR:Q71QF9; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0031965; C:nuclear membrane; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0035904; P:aorta development; ISO:RGD.
DR   GO; GO:0060976; P:coronary vasculature development; ISO:RGD.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR   GO; GO:2000691; P:negative regulation of cardiac muscle cell myoblast differentiation; ISO:RGD.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR   GO; GO:0001843; P:neural tube closure; ISO:RGD.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:RGD.
DR   GO; GO:0006606; P:protein import into nucleus; IDA:RGD.
DR   CDD; cd09418; LIM2_Prickle; 1.
DR   CDD; cd09420; LIM3_Prickle; 1.
DR   CDD; cd09827; PET_Prickle; 1.
DR   InterPro; IPR033726; LIM2_prickle.
DR   InterPro; IPR033727; LIM3_prickle.
DR   InterPro; IPR010442; PET_domain.
DR   InterPro; IPR033723; PET_prickle.
DR   InterPro; IPR001781; Znf_LIM.
DR   Pfam; PF00412; LIM; 3.
DR   Pfam; PF06297; PET; 1.
DR   SMART; SM00132; LIM; 3.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR   PROSITE; PS51303; PET; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; LIM domain; Lipoprotein; Membrane; Metal-binding; Methylation;
KW   Nucleus; Phosphoprotein; Prenylation; Reference proteome; Repeat; Zinc.
FT   CHAIN           1..828
FT                   /note="Prickle-like protein 1"
FT                   /id="PRO_0000075890"
FT   PROPEP          829..831
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000396714"
FT   DOMAIN          14..122
FT                   /note="PET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00636"
FT   DOMAIN          124..189
FT                   /note="LIM zinc-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          189..249
FT                   /note="LIM zinc-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          249..313
FT                   /note="LIM zinc-binding 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   REGION          314..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          664..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          763..831
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        792..813
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        814..831
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         315
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3U5C7"
FT   MOD_RES         591
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3U5C7"
FT   MOD_RES         594
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3U5C7"
FT   MOD_RES         683
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3U5C7"
FT   MOD_RES         828
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           828
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        115
FT                   /note="K -> I (in Ref. 1; AW434734)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        121
FT                   /note="M -> T (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        125
FT                   /note="V -> L (in Ref. 1; AW434734)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        133
FT                   /note="M -> I (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   831 AA;  94170 MW;  25B999F11055FBD1 CRC64;
     MPLEMEPKMS KLAFGCQRSS TSDDDSGCAL EEYAWVPPGL RPEQIQLYFA CLPEEKVPYV
     NSPGEKHRIK QLLYQLPPHD NEVRYCQSLS EEEKKELQVF SAQRKKEALG RGTIKLLSRA
     MMHAVCEQCG LQMNGGEVAV FASRAGPGVC WRPSCFVCFT CNELLVDLIY FYQDGKIHCG
     RHHAELLKPR CSACDEIIFA DECTEAEGRH WHMKHFCCLE CETVLGGQRY IMKDGRPFCC
     GCFESLYAEY CETCGEHIGV DHAQMTYDGQ HWHATEACFS CAQCKASLLG CPFLPKQGQI
     YCSKTCSLGE DIHASDSSDS AFQSARSRDS RRSVRMGRSS RSADQCRQSL LLSPALNYKF
     PGLSGSADDT LSRKLDDVSL SGQGAGFAHE EFWKARVDQE ASEDPEEWAE HEDYMTQLLL
     KFGDKNLFQQ PPSEVDMRAS EHWIPDNMVT NKPEAKQNHQ SLASKKYQSD MYWAQSQDGL
     GDSAYGSHPG PASSRRLQEL DLDHGAAGYN HDQTQWYEDS LECLSDLKPE QSVRDSMDSL
     ALSNITGASV DGESKPRPSL YSLQNFEEIE AEDCEKMSNM GTLNSSMLHR SAESLKSLNS
     ELCPEKIIPE EKPVHLPVLR RSKSQSRPQQ VKFSDDVIDN GSYDIEIRQP PMSERTRRRV
     YHFEERGSRP HHHRHRRSRK SRSDNALNLV TERKYSAKDR LRLYTPDNYE KFIQSKGARE
     LQAYMQNANL YGQYAHTTSD YALQNPGMTR FLGLYGDDDD SWCSSSTSSS DSEEEGYFLG
     QPIPQPRPQR FTYYTDDLSS PASALPTPQF NQRTTKSKKK KGHRGKNCII S
 
 
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