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RINI_MOUSE
ID   RINI_MOUSE              Reviewed;         456 AA.
AC   Q91VI7; Q924P4;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Ribonuclease inhibitor;
DE   AltName: Full=Ribonuclease/angiogenin inhibitor 1;
GN   Name=Rnh1; Synonyms=Rnh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Melnick M.B., Comb M.J.;
RT   "Mouse homolog of ribonuclease/angiogenesis inhibitor.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NMRI; TISSUE=Mammary tumor;
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).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG.
CC       May play a role in redox homeostasis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms high-affinity heterodimers with RNASE1, ANG and RNASE2.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; AF071546; AAK68859.1; -; mRNA.
DR   EMBL; AK133822; BAE21862.1; -; mRNA.
DR   EMBL; AK141351; BAE24659.1; -; mRNA.
DR   EMBL; AK147059; BAE27643.1; -; mRNA.
DR   EMBL; BC010331; AAH10331.1; -; mRNA.
DR   CCDS; CCDS22002.1; -.
DR   RefSeq; NP_001165571.1; NM_001172100.1.
DR   RefSeq; NP_001165572.1; NM_001172101.1.
DR   RefSeq; NP_660117.2; NM_145135.3.
DR   PDB; 3TSR; X-ray; 2.20 A; E/F/G/H=1-456.
DR   PDBsum; 3TSR; -.
DR   AlphaFoldDB; Q91VI7; -.
DR   SMR; Q91VI7; -.
DR   BioGRID; 223500; 14.
DR   IntAct; Q91VI7; 4.
DR   MINT; Q91VI7; -.
DR   STRING; 10090.ENSMUSP00000101651; -.
DR   iPTMnet; Q91VI7; -.
DR   PhosphoSitePlus; Q91VI7; -.
DR   SwissPalm; Q91VI7; -.
DR   UCD-2DPAGE; Q91VI7; -.
DR   CPTAC; non-CPTAC-3997; -.
DR   EPD; Q91VI7; -.
DR   jPOST; Q91VI7; -.
DR   MaxQB; Q91VI7; -.
DR   PaxDb; Q91VI7; -.
DR   PeptideAtlas; Q91VI7; -.
DR   PRIDE; Q91VI7; -.
DR   ProteomicsDB; 255277; -.
DR   Antibodypedia; 22490; 474 antibodies from 31 providers.
DR   DNASU; 107702; -.
DR   Ensembl; ENSMUST00000106033; ENSMUSP00000101651; ENSMUSG00000038650.
DR   Ensembl; ENSMUST00000167493; ENSMUSP00000133061; ENSMUSG00000038650.
DR   GeneID; 107702; -.
DR   KEGG; mmu:107702; -.
DR   UCSC; uc009kjs.2; mouse.
DR   CTD; 6050; -.
DR   MGI; MGI:1195456; Rnh1.
DR   VEuPathDB; HostDB:ENSMUSG00000038650; -.
DR   eggNOG; KOG4308; Eukaryota.
DR   GeneTree; ENSGT00940000161492; -.
DR   HOGENOM; CLU_002274_4_6_1; -.
DR   InParanoid; Q91VI7; -.
DR   OMA; GGNDIHA; -.
DR   OrthoDB; 710473at2759; -.
DR   PhylomeDB; Q91VI7; -.
DR   BioGRID-ORCS; 107702; 4 hits in 70 CRISPR screens.
DR   ChiTaRS; Rnh1; mouse.
DR   PRO; PR:Q91VI7; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q91VI7; protein.
DR   Bgee; ENSMUSG00000038650; Expressed in vault of skull and 264 other tissues.
DR   ExpressionAtlas; Q91VI7; baseline and differential.
DR   Genevisible; Q91VI7; MM.
DR   GO; GO:0032311; C:angiogenin-PRI complex; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0008428; F:ribonuclease inhibitor activity; ISO:MGI.
DR   GO; GO:0045765; P:regulation of angiogenesis; ISO:MGI.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR001611; Leu-rich_rpt.
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.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Leucine-rich repeat; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..456
FT                   /note="Ribonuclease inhibitor"
FT                   /id="PRO_0000097344"
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        11
FT                   /note="S -> G (in Ref. 1; AAK68859)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68
FT                   /note="V -> A (in Ref. 1; AAK68859)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        254
FT                   /note="R -> G (in Ref. 1; AAK68859)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        278
FT                   /note="K -> N (in Ref. 1; AAK68859)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        448
FT                   /note="E -> G (in Ref. 1; AAK68859)"
FT                   /evidence="ECO:0000305"
FT   STRAND          1..7
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           12..22
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          26..33
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           37..39
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           40..48
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           64..74
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           94..99
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           100..106
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           121..132
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          140..143
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           151..153
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           154..163
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          169..171
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           178..191
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          198..200
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           208..210
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           211..220
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          226..228
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          231..233
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           235..246
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          255..257
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           265..277
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          283..285
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           292..303
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          312..314
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           322..324
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           325..334
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          340..342
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           349..360
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          369..371
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           379..381
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           382..391
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          397..399
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           407..417
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          426..428
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           436..448
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          453..455
FT                   /evidence="ECO:0007829|PDB:3TSR"
SQ   SEQUENCE   456 AA;  49816 MW;  007B782F05A357E8 CRC64;
     MSLDIQCEQL SDARWTELLP LIQQYEVVRL DDCGLTEVRC KDISSAVQAN PALTELSLRT
     NELGDGGVGL VLQGLQNPTC KIQKLSLQNC GLTEAGCGIL PGMLRSLSTL RELHLNDNPM
     GDAGLKLLCE GLQDPQCRLE KLQLEYCNLT ATSCEPLASV LRVKADFKEL VLSNNDLHEP
     GVRILCQGLK DSACQLESLK LENCGITAAN CKDLCDVVAS KASLQELDLS SNKLGNAGIA
     ALCPGLLLPS CKLRTLWLWE CDITAEGCKD LCRVLRAKQS LKELSLASNE LKDEGARLLC
     ESLLEPGCQL ESLWIKTCSL TAASCPYFCS VLTKSRSLLE LQMSSNPLGD EGVQELCKAL
     SQPDTVLREL WLGDCDVTNS GCSSLANVLL ANRSLRELDL SNNCMGGPGV LQLLESLKQP
     SCTLQQLVLY DIYWTNEVEE QLRALEEERP SLRIIS
 
 
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