CRIP1_RAT
ID CRIP1_RAT Reviewed; 77 AA.
AC P63255; P04006;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Cysteine-rich protein 1;
DE Short=CRP-1;
DE AltName: Full=Cysteine-rich intestinal protein;
DE Short=CRIP;
GN Name=Crip1; Synonyms=Crip;
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;
RX PubMed=3085096; DOI=10.1073/pnas.83.8.2516;
RA Birkenmeier E.H., Gordon J.I.;
RT "Developmental regulation of a gene that encodes a cysteine-rich intestinal
RT protein and maps near the murine immunoglobulin heavy chain locus.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:2516-2520(1986).
RN [2]
RP PROTEIN SEQUENCE OF 2-41, AND ZINC-BINDING.
RC STRAIN=Sprague-Dawley; TISSUE=Intestine;
RX PubMed=1946385; DOI=10.1073/pnas.88.21.9671;
RA Hempe J.M., Cousins R.J.;
RT "Cysteine-rich intestinal protein binds zinc during transmucosal zinc
RT transport.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9671-9674(1991).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=8632452; DOI=10.1006/jmbi.1996.0153;
RA Perez-Alvarado G.C., Kosa J.L., Louis H.A., Beckerle M.C., Winge D.R.,
RA Summers M.F.;
RT "Structure of the cysteine-rich intestinal protein, CRIP.";
RL J. Mol. Biol. 257:153-174(1996).
CC -!- FUNCTION: Seems to have a role in zinc absorption and may function as
CC an intracellular zinc transport protein.
CC -!- DEVELOPMENTAL STAGE: The concentration in intestinal tissues undergoes
CC an abrupt increase during the animal's transition from suckling to
CC weaning.
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DR PIR; A03270; GYRTI.
DR RefSeq; NP_001128405.1; NM_001134933.2.
DR RefSeq; NP_001231796.1; NM_001244867.1.
DR PDB; 1IML; NMR; -; A=2-77.
DR PDBsum; 1IML; -.
DR AlphaFoldDB; P63255; -.
DR SMR; P63255; -.
DR STRING; 10116.ENSRNOP00000006835; -.
DR iPTMnet; P63255; -.
DR PhosphoSitePlus; P63255; -.
DR jPOST; P63255; -.
DR PaxDb; P63255; -.
DR PRIDE; P63255; -.
DR Ensembl; ENSRNOT00000006835; ENSRNOP00000006835; ENSRNOG00000027990.
DR GeneID; 691657; -.
DR KEGG; rno:691657; -.
DR CTD; 1396; -.
DR RGD; 1597237; Crip1.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000162342; -.
DR HOGENOM; CLU_026811_4_1_1; -.
DR InParanoid; P63255; -.
DR OMA; CHNPCYS; -.
DR OrthoDB; 1214165at2759; -.
DR PhylomeDB; P63255; -.
DR EvolutionaryTrace; P63255; -.
DR PRO; PR:P63255; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000027990; Expressed in jejunum and 19 other tissues.
DR Genevisible; P63255; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0042277; F:peptide binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0071236; P:cellular response to antibiotic; ISS:UniProtKB.
DR GO; GO:0071493; P:cellular response to UV-B; ISS:UniProtKB.
DR GO; GO:0006955; P:immune response; ISO:RGD.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISS:UniProtKB.
DR GO; GO:0060741; P:prostate gland stromal morphogenesis; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0010033; P:response to organic substance; ISO:RGD.
DR GO; GO:0010043; P:response to zinc ion; ISS:UniProtKB.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00132; LIM; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; LIM domain;
KW Metal-binding; Methylation; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1946385"
FT CHAIN 2..77
FT /note="Cysteine-rich protein 1"
FT /id="PRO_0000075709"
FT DOMAIN 2..63
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50238"
FT MOD_RES 22
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63254"
FT MOD_RES 68
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P63254"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:1IML"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1IML"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1IML"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:1IML"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1IML"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:1IML"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1IML"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:1IML"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1IML"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1IML"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:1IML"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1IML"
SQ SEQUENCE 77 AA; 8550 MW; BBE8E17A19352EC1 CRC64;
MPKCPKCDKE VYFAERVTSL GKDWHRPCLK CEKCGKTLTS GGHAEHEGKP YCNHPCYSAM
FGPKGFGRGG AESHTFK
