RINI_PIG
ID RINI_PIG Reviewed; 456 AA.
AC P10775;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ribonuclease inhibitor;
DE AltName: Full=Ribonuclease/angiogenin inhibitor 1;
GN Name=RNH1; Synonyms=RI, RNH;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC TISSUE=Liver;
RX PubMed=3219361; DOI=10.1021/bi00423a006;
RA Hofsteenge J., Kieffer B., Matthies R., Hemmings B.A., Stone S.R.;
RT "Amino acid sequence of the ribonuclease inhibitor from porcine liver
RT reveals the presence of leucine-rich repeats.";
RL Biochemistry 27:8537-8544(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 82-456, FUNCTION, AND SUBUNIT.
RC TISSUE=Kidney;
RX PubMed=2271559; DOI=10.1021/bi00489a046;
RA Vicentini A.M., Kieffer B., Matthies R., Meyhack B., Hemmings B.A.,
RA Stone S.R., Hofsteenge J.;
RT "Protein chemical and kinetic characterization of recombinant porcine
RT ribonuclease inhibitor expressed in Saccharomyces cerevisiae.";
RL Biochemistry 29:8827-8834(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=8264799; DOI=10.1038/366751a0;
RA Kobe B., Deisenhofer J.;
RT "Crystal structure of porcine ribonuclease inhibitor, a protein with
RT leucine-rich repeats.";
RL Nature 366:751-756(1993).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=7877692; DOI=10.1038/374183a0;
RA Kobe B., Deisenhofer J.;
RT "A structural basis of the interactions between leucine-rich repeats and
RT protein ligands.";
RL Nature 374:183-186(1995).
CC -!- FUNCTION: Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG.
CC May play a role in redox homeostasis. {ECO:0000269|PubMed:2271559}.
CC -!- SUBUNIT: Forms high-affinity heterodimers with RNASE1, ANG and RNASE2.
CC {ECO:0000269|PubMed:2271559}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: The LRR domain forms a horseshoe-shaped structure that
CC interacts tightly with target RNases via a large protein interaction
CC surface on its interior side. {ECO:0000250}.
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DR EMBL; M58700; AAA63448.1; -; mRNA.
DR PIR; A31857; A31857.
DR RefSeq; XP_013847653.1; XM_013992199.1.
DR PDB; 1DFJ; X-ray; 2.50 A; I=1-456.
DR PDB; 2BNH; X-ray; 2.30 A; A=1-456.
DR PDBsum; 1DFJ; -.
DR PDBsum; 2BNH; -.
DR AlphaFoldDB; P10775; -.
DR SMR; P10775; -.
DR IntAct; P10775; 1.
DR MINT; P10775; -.
DR iPTMnet; P10775; -.
DR PeptideAtlas; P10775; -.
DR PRIDE; P10775; -.
DR Ensembl; ENSSSCT00055003614; ENSSSCP00055002749; ENSSSCG00055001944.
DR Ensembl; ENSSSCT00055003629; ENSSSCP00055002762; ENSSSCG00055001944.
DR Ensembl; ENSSSCT00055003640; ENSSSCP00055002773; ENSSSCG00055001944.
DR Ensembl; ENSSSCT00055003675; ENSSSCP00055002805; ENSSSCG00055001944.
DR Ensembl; ENSSSCT00070055317; ENSSSCP00070046958; ENSSSCG00070027590.
DR Ensembl; ENSSSCT00070055321; ENSSSCP00070046962; ENSSSCG00070027590.
DR InParanoid; P10775; -.
DR OMA; GGNDIHA; -.
DR EvolutionaryTrace; P10775; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 2.
DR GO; GO:0032311; C:angiogenin-PRI complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0008428; F:ribonuclease inhibitor activity; IBA:GO_Central.
DR GO; GO:0045765; P:regulation of angiogenesis; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR041302; LRR_RI_cap.
DR Pfam; PF13516; LRR_6; 7.
DR Pfam; PF18779; LRR_RI_capping; 1.
DR SMART; SM00367; LRR_CC; 6.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Leucine-rich repeat; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..456
FT /note="Ribonuclease inhibitor"
FT /id="PRO_0000097346"
FT REPEAT 15..43
FT /note="LRR 1"
FT REPEAT 44..71
FT /note="LRR 2"
FT REPEAT 72..100
FT /note="LRR 3"
FT REPEAT 101..128
FT /note="LRR 4"
FT REPEAT 129..157
FT /note="LRR 5"
FT REPEAT 158..185
FT /note="LRR 6"
FT REPEAT 186..214
FT /note="LRR 7"
FT REPEAT 215..242
FT /note="LRR 8"
FT REPEAT 243..271
FT /note="LRR 9"
FT REPEAT 272..299
FT /note="LRR 10"
FT REPEAT 300..328
FT /note="LRR 11"
FT REPEAT 329..356
FT /note="LRR 12"
FT REPEAT 357..385
FT /note="LRR 13"
FT REPEAT 386..413
FT /note="LRR 14"
FT REPEAT 414..442
FT /note="LRR 15"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:3219361"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13489"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:2BNH"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:2BNH"
FT HELIX 37..47
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:2BNH"
FT HELIX 64..75
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2BNH"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:2BNH"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2BNH"
FT HELIX 121..133
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:2BNH"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:2BNH"
FT HELIX 178..190
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:2BNH"
FT HELIX 208..220
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:2BNH"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:2BNH"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:2BNH"
FT HELIX 292..303
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:2BNH"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:2BNH"
FT HELIX 325..334
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:2BNH"
FT HELIX 349..359
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:2BNH"
FT HELIX 379..391
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:1DFJ"
FT HELIX 407..417
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:2BNH"
FT HELIX 436..448
FT /evidence="ECO:0007829|PDB:2BNH"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:2BNH"
SQ SEQUENCE 456 AA; 49023 MW; 01DA0A529CDC763E CRC64;
MNLDIHCEQL SDARWTELLP LLQQYEVVRL DDCGLTEEHC KDIGSALRAN PSLTELCLRT
NELGDAGVHL VLQGLQSPTC KIQKLSLQNC SLTEAGCGVL PSTLRSLPTL RELHLSDNPL
GDAGLRLLCE GLLDPQCHLE KLQLEYCRLT AASCEPLASV LRATRALKEL TVSNNDIGEA
GARVLGQGLA DSACQLETLR LENCGLTPAN CKDLCGIVAS QASLRELDLG SNGLGDAGIA
ELCPGLLSPA SRLKTLWLWE CDITASGCRD LCRVLQAKET LKELSLAGNK LGDEGARLLC
ESLLQPGCQL ESLWVKSCSL TAACCQHVSL MLTQNKHLLE LQLSSNKLGD SGIQELCQAL
SQPGTTLRVL CLGDCEVTNS GCSSLASLLL ANRSLRELDL SNNCVGDPGV LQLLGSLEQP
GCALEQLVLY DTYWTEEVED RLQALEGSKP GLRVIS
