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RIN3_MOUSE
ID   RIN3_MOUSE              Reviewed;         980 AA.
AC   P59729; B2RQF8;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Ras and Rab interactor 3;
DE   AltName: Full=Ras interaction/interference protein 3;
GN   Name=Rin3;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Liver, Lung, and Spleen;
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: Ras effector protein that functions as a guanine nucleotide
CC       exchange (GEF) for RAB5B and RAB31, by exchanging bound GDP for free
CC       GTP. Required for normal RAB31 function (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CD2AP, RAB5B, RAB31 and BIN1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TB24}.
CC       Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q8TB24}. Early endosome
CC       {ECO:0000250|UniProtKB:Q8TB24}. Note=Activation of tyrosine
CC       phosphorylation signaling induces translocation to cytoplasmic
CC       vesicles. {ECO:0000250|UniProtKB:Q8TB24}.
CC   -!- SIMILARITY: Belongs to the RIN (Ras interaction/interference) family.
CC       {ECO:0000305}.
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DR   EMBL; AK032205; BAC27757.1; -; mRNA.
DR   EMBL; BC137907; AAI37908.1; -; mRNA.
DR   CCDS; CCDS26118.1; -.
DR   RefSeq; NP_808288.2; NM_177620.4.
DR   AlphaFoldDB; P59729; -.
DR   SMR; P59729; -.
DR   BioGRID; 229966; 5.
DR   STRING; 10090.ENSMUSP00000060771; -.
DR   iPTMnet; P59729; -.
DR   PhosphoSitePlus; P59729; -.
DR   EPD; P59729; -.
DR   jPOST; P59729; -.
DR   MaxQB; P59729; -.
DR   PaxDb; P59729; -.
DR   PRIDE; P59729; -.
DR   ProteomicsDB; 254884; -.
DR   Antibodypedia; 26773; 89 antibodies from 23 providers.
DR   DNASU; 217835; -.
DR   Ensembl; ENSMUST00000056950; ENSMUSP00000060771; ENSMUSG00000044456.
DR   GeneID; 217835; -.
DR   KEGG; mmu:217835; -.
DR   UCSC; uc007ouc.2; mouse.
DR   CTD; 79890; -.
DR   MGI; MGI:2385708; Rin3.
DR   VEuPathDB; HostDB:ENSMUSG00000044456; -.
DR   eggNOG; KOG2320; Eukaryota.
DR   GeneTree; ENSGT00940000158622; -.
DR   InParanoid; P59729; -.
DR   OMA; YCFVYHP; -.
DR   OrthoDB; 251004at2759; -.
DR   PhylomeDB; P59729; -.
DR   TreeFam; TF331067; -.
DR   Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   BioGRID-ORCS; 217835; 2 hits in 70 CRISPR screens.
DR   ChiTaRS; Rin3; mouse.
DR   PRO; PR:P59729; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; P59729; protein.
DR   Bgee; ENSMUSG00000044456; Expressed in granulocyte and 146 other tissues.
DR   ExpressionAtlas; P59729; baseline and differential.
DR   Genevisible; P59729; MM.
DR   GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0030425; C:dendrite; IDA:ARUK-UCL.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0030139; C:endocytic vesicle; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR   GO; GO:0031982; C:vesicle; ISO:MGI.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR   GO; GO:0060755; P:negative regulation of mast cell chemotaxis; ISO:MGI.
DR   GO; GO:0002091; P:negative regulation of receptor internalization; ISO:MGI.
DR   GO; GO:0097494; P:regulation of vesicle size; ISO:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   CDD; cd10395; SH2_RIN3; 1.
DR   Gene3D; 1.20.1050.80; -; 1.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR035869; RIN3_SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR003123; VPS9.
DR   InterPro; IPR045046; Vps9-like.
DR   InterPro; IPR037191; VPS9_dom_sf.
DR   PANTHER; PTHR23101; PTHR23101; 1.
DR   Pfam; PF02204; VPS9; 1.
DR   SMART; SM00314; RA; 1.
DR   SMART; SM00167; VPS9; 1.
DR   SUPFAM; SSF109993; SSF109993; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS51205; VPS9; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoplasmic vesicle; Endosome; GTPase activation;
KW   Reference proteome; SH2 domain.
FT   CHAIN           1..980
FT                   /note="Ras and Rab interactor 3"
FT                   /id="PRO_0000191323"
FT   DOMAIN          63..158
FT                   /note="SH2"
FT   DOMAIN          700..843
FT                   /note="VPS9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT   DOMAIN          865..962
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          509..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..729
FT                   /note="Interaction with RAB5B"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        20..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..262
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..307
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..375
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..558
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        288
FT                   /note="T -> I (in Ref. 1; BAC27757)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        332
FT                   /note="T -> K (in Ref. 1; BAC27757)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        560
FT                   /note="S -> T (in Ref. 1; BAC27757)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        563..565
FT                   /note="NVK -> DVE (in Ref. 1; BAC27757)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   980 AA;  107220 MW;  F803A8CFEE17A7B8 CRC64;
     MRRAEAPSSA HPAGPIPDAG KGEGEEDEEK DGTRLGLSTT PRNCIPRRGI SVLEKLVKTC
     PVWLQLGLGQ AEAAKILQQE MAGMFLVCRD NNLKQLVLCV HFPSLKGSSA EVLEYPIKEE
     KAILYLEGSV LVFEDIFRLI AFYCVSRDLL PFTLRLPQAI LEASSFLELE TISNLGLGFW
     DSSLNSRGSA EPLRSPAPGT PASSSLRPTT HYANCSCEIE LSVGNDRLWF VNPIFIEDCI
     LPADPPPLPT GSYPPRPTPA TPDATSPTSK GSPRRPPPPP PLPTVPPTGP ARPLAPPVPP
     AGPLPNSPLT PTSHLAPHAP GPPGHSNQPP MTACESLPRP AVGLGPFGEE EMKPGTTPNP
     LHQAPPPPLP LKKALPAAPP RRRISERVSL ESQNVGTSTD RDHSGISRTA SLNLPPQSTV
     SSLGDRPPRT TEQSQDTEAK ASHADSIPVP PGKAKQPPVP PPRKKRVSRQ LASTLLSPLE
     SPIQEASSEK QATGASWEGL SPVRQAGMQH LQVQSSSCPQ SSPEFKGSQA SLSDSLGVPA
     SAADQDSYST SSAEEELEFS SPNVKKKPSM ILDKARHRLS FVSFASVFHA FLSSDRKLYK
     KVVELAQDKS SYFGSLVQDY KVYSLEMMAR QTSSTEMLQE IRTMMTQLKS YLLQSTELKA
     LVEPTLHSEE ELEAIVESAL YKCVLKPLKE AINSSLLEIH SRDGSLQQLK ENQLVVLATT
     TTDLGVTTSV PEVAVMEKIL QKLTSMHKAY SPGKKISILL KTCKLIYDSM ALGNPGKPYG
     ADDFLPVLMY VLARSNLTEM LLNVEYMMEL MDPALQLGEG SYYLTTTYGA LEHIKNYDKI
     TVTRQLSVEV QDSIHRWERR RTLNKARASR SSVQDFICVS YLKPEQQSRT LASRADTAAQ
     ALCAQCAEKF EVSQPQDYRL FVLVDGRCFQ LADEALPHRI KGYLLRSEPK RDFHFVYRPQ
     DSGKDASSQP CIVVREPNFL
 
 
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