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CSRP1_PONAB
ID   CSRP1_PONAB             Reviewed;         193 AA.
AC   Q5RCT4;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Cysteine and glycine-rich protein 1;
DE   AltName: Full=Cysteine-rich protein 1;
DE            Short=CRP1;
GN   Name=CSRP1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Could play a role in neuronal development. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ASCC1; ASCC2 AND TRIP4.
CC       {ECO:0000250|UniProtKB:P21291}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P21291}.
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DR   EMBL; CR858184; CAH90423.1; -; mRNA.
DR   RefSeq; NP_001125211.1; NM_001131739.1.
DR   AlphaFoldDB; Q5RCT4; -.
DR   SMR; Q5RCT4; -.
DR   STRING; 9601.ENSPPYP00000000406; -.
DR   GeneID; 100172103; -.
DR   KEGG; pon:100172103; -.
DR   CTD; 1465; -.
DR   eggNOG; KOG1700; Eukaryota.
DR   InParanoid; Q5RCT4; -.
DR   OrthoDB; 1214165at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001781; Znf_LIM.
DR   Pfam; PF00412; LIM; 2.
DR   SMART; SM00132; LIM; 2.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; Isopeptide bond; LIM domain; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Zinc.
FT   CHAIN           1..193
FT                   /note="Cysteine and glycine-rich protein 1"
FT                   /id="PRO_0000075717"
FT   DOMAIN          10..61
FT                   /note="LIM zinc-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          119..170
FT                   /note="LIM zinc-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   MOTIF           64..69
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         81
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47875"
FT   MOD_RES         84
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P97315"
FT   MOD_RES         112
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P21291"
FT   MOD_RES         131
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P21291"
FT   MOD_RES         137
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P97315"
FT   MOD_RES         161
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P97315"
FT   MOD_RES         192
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21291"
FT   CROSSLNK        91
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P21291"
SQ   SEQUENCE   193 AA;  20583 MW;  3D1369DB248F48E3 CRC64;
     MPNWGGGKKC GVCQKTVYFA EEVQCEGNSF HKSCFLCMVC KKNLDSTTVA VHGEEIYCKS
     CYGKKYGPKG YGYGQGAGTL STDKGESLGI KHEESPGHRP TTNPNASKFA QKIGGSERCP
     RCSQAVYAAE KVIGAGKSWH KACFRCAKCG KGLESTTLAD KDGEIYCKGC YAKNFGPKGF
     GFGQGAGALV HSE
 
 
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