ID RINI_RAT Reviewed; 456 AA.
AC P29315; Q6IRS9;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 2.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=Ribonuclease inhibitor;
DE AltName: Full=Ribonuclease/angiogenin inhibitor 1;
GN Name=Rnh1; Synonyms=Rnh;
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], PROTEIN SEQUENCE OF 42-64; 66-78; 169-190;
RP 293-309 AND 335-349, FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=1536887; DOI=10.1016/0167-4781(92)90513-y;
RA Kawanomoto M., Motojima K., Sasaki M., Hattori H., Goto S.;
RT "cDNA cloning and sequence of rat ribonuclease inhibitor, and tissue
RT distribution of the mRNA.";
RL Biochim. Biophys. Acta 1129:335-338(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
CC -!- FUNCTION: Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG.
CC May play a role in redox homeostasis. {ECO:0000269|PubMed:1536887}.
CC -!- SUBUNIT: Forms high-affinity heterodimers with RNASE1, ANG and RNASE2.
CC {ECO:0000269|PubMed:1536887}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Brain, heart, lung, liver, spleen, testes and
CC kidney; highest in the lung and lowest in the heart.
CC {ECO:0000269|PubMed:1536887}.
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; X62528; CAA44388.1; -; mRNA.
DR EMBL; BC070501; AAH70501.1; -; mRNA.
DR PIR; S20597; S20597.
DR RefSeq; NP_001257691.1; NM_001270762.1.
DR RefSeq; NP_001257692.1; NM_001270763.1.
DR RefSeq; NP_620805.2; NM_139105.3.
DR AlphaFoldDB; P29315; -.
DR SMR; P29315; -.
DR IntAct; P29315; 1.
DR STRING; 10116.ENSRNOP00000074961; -.
DR iPTMnet; P29315; -.
DR PhosphoSitePlus; P29315; -.
DR jPOST; P29315; -.
DR PaxDb; 10116-ENSRNOP00000022241; -.
DR GeneID; 100360501; -.
DR KEGG; rno:100360501; -.
DR AGR; RGD:621398; -.
DR CTD; 6050; -.
DR RGD; 621398; Rnh1.
DR eggNOG; KOG4308; Eukaryota.
DR InParanoid; P29315; -.
DR OrthoDB; 55870at2759; -.
DR PhylomeDB; P29315; -.
DR PRO; PR:P29315; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0032311; C:angiogenin-PRI complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008428; F:ribonuclease inhibitor activity; ISO:RGD.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0045765; P:regulation of angiogenesis; ISO:RGD.
DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR CDD; cd00116; LRR_RI; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR041302; LRR_RI_cap.
DR PANTHER; PTHR45690; NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 12; 1.
DR PANTHER; PTHR45690:SF15; NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 14; 1.
DR Pfam; PF13516; LRR_6; 7.
DR Pfam; PF18779; LRR_RI_capping; 1.
DR SMART; SM00368; LRR_RI; 13.
DR SUPFAM; SSF52047; RNI-like; 2.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Leucine-rich repeat;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..456
FT /note="Ribonuclease inhibitor"
FT /id="PRO_0000097347"
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:0000250|UniProtKB:P10775"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13489"
FT CONFLICT 336
FT /note="R -> S (in Ref. 1; CAA44388)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="N -> T (in Ref. 2; AAH70501)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="I -> A (in Ref. 2; AAH70501)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 49974 MW; 85A8E4B1F09E5898 CRC64;
MSLDIQCEQL SDARWTELLP LIQQYQVVRL DDCGLTEVRC KDIRSAIQAN PALTELSLRT
NELGDAGVGL VLQGLQNPTC KIQKLSLQNC SLTEAGCGVL PDVLRSLSTL RELHLNDNPL
GDEGLKLLCE GLRDPQCRLE KLQLEYCNLT ATSCEPLASV LRVKPDFKEL VLSNNDFHEA
GIHTLCQGLK DSACQLESLK LENCGITSAN CKDLCDVVAS KASLQELDLG SNKLGNTGIA
ALCSGLLLPS CRLRTLWLWD CDVTAEGCKD LCRVLRAKQS LKELSLAGNE LKDEGAQLLC
ESLLEPGCQL ESLWVKTCSL TAASCPHFCS VLTKNRSLFE LQMSSNPLGD SGVVELCKAL
GYPDTVLRVL WLGDCDVTDS GCSSLATVLL ANRSLRELDL SNNCMGDNGV LQLLESLKQP
SCILQQLVLY DIYWTDEVED QLRALEEERP SLRIIS
//
