位置:首页 > 蛋白库 > SNX8_MOUSE
SNX8_MOUSE
ID   SNX8_MOUSE              Reviewed;         459 AA.
AC   Q8CFD4; Q8BLI6; Q8BUQ7;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Sorting nexin-8;
GN   Name=Snx8;
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=FVB/N; 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-459.
RC   STRAIN=C57BL/6J;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, 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: May be involved in several stages of intracellular
CC       trafficking. May play a role in intracellular protein transport from
CC       early endosomes to the trans-Golgi network (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC       Note=Colocalizes with retromer components. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32202.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE28549.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC037599; AAH37599.1; -; mRNA.
DR   EMBL; AK045061; BAC32202.1; ALT_INIT; mRNA.
DR   EMBL; AK082871; BAC38662.1; -; mRNA.
DR   EMBL; AK148429; BAE28549.1; ALT_INIT; mRNA.
DR   CCDS; CCDS39356.1; -.
DR   RefSeq; NP_758481.1; NM_172277.3.
DR   AlphaFoldDB; Q8CFD4; -.
DR   SMR; Q8CFD4; -.
DR   BioGRID; 231175; 4.
DR   IntAct; Q8CFD4; 2.
DR   MINT; Q8CFD4; -.
DR   STRING; 10090.ENSMUSP00000031539; -.
DR   iPTMnet; Q8CFD4; -.
DR   PhosphoSitePlus; Q8CFD4; -.
DR   EPD; Q8CFD4; -.
DR   MaxQB; Q8CFD4; -.
DR   PaxDb; Q8CFD4; -.
DR   PeptideAtlas; Q8CFD4; -.
DR   PRIDE; Q8CFD4; -.
DR   ProteomicsDB; 261545; -.
DR   Antibodypedia; 24341; 290 antibodies from 28 providers.
DR   DNASU; 231834; -.
DR   Ensembl; ENSMUST00000031539; ENSMUSP00000031539; ENSMUSG00000029560.
DR   GeneID; 231834; -.
DR   KEGG; mmu:231834; -.
DR   UCSC; uc009ahp.1; mouse.
DR   CTD; 29886; -.
DR   MGI; MGI:2443816; Snx8.
DR   VEuPathDB; HostDB:ENSMUSG00000029560; -.
DR   eggNOG; KOG2273; Eukaryota.
DR   GeneTree; ENSGT00460000041594; -.
DR   InParanoid; Q8CFD4; -.
DR   OrthoDB; 793604at2759; -.
DR   PhylomeDB; Q8CFD4; -.
DR   TreeFam; TF314082; -.
DR   BioGRID-ORCS; 231834; 1 hit in 73 CRISPR screens.
DR   ChiTaRS; Snx8; mouse.
DR   PRO; PR:Q8CFD4; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q8CFD4; protein.
DR   Bgee; ENSMUSG00000029560; Expressed in yolk sac and 206 other tissues.
DR   ExpressionAtlas; Q8CFD4; baseline and differential.
DR   Genevisible; Q8CFD4; MM.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0030904; C:retromer complex; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR   GO; GO:0034498; P:early endosome to Golgi transport; ISS:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR   CDD; cd06866; PX_SNX8_Mvp1p_like; 1.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   Gene3D; 3.30.1520.10; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR028662; SNX8/Mvp1.
DR   InterPro; IPR035704; SNX8/Mvp1_PX.
DR   InterPro; IPR045734; Snx8_BAR_dom.
DR   PANTHER; PTHR46571; PTHR46571; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF19566; Snx8_BAR_dom; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; SSF64268; 1.
DR   PROSITE; PS50195; PX; 1.
PE   1: Evidence at protein level;
KW   Endosome; Lipid-binding; Membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..459
FT                   /note="Sorting nexin-8"
FT                   /id="PRO_0000236199"
FT   DOMAIN          68..176
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         104
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-3-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58088"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-3-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58088"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-3-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58088"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         446
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5X2"
FT   MOD_RES         450
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        222
FT                   /note="N -> Y (in Ref. 2; BAC38662)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        366
FT                   /note="L -> V (in Ref. 2; BAC38662)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   459 AA;  52059 MW;  5E0BE9C1AB054454 CRC64;
     MTGRAMDPLP SPAVAAAAEA EADEEADPPA TGPRTSQVTE WRALDPGRMQ MPQGNPLLLS
     YTLQELLAKD TVQVELIPEK KGLFLKHVEY EVSSQRFKSS VYRRYNDFVV FHEVLLHKFP
     YRMVPALPPK RVLGADREFI EGRRRALKRF INLVARHPPF SEDVLLKLFL SFSGSDVQHK
     LKEAAQCVGD EFMNCKLAAR AKDFLPADIQ TQFAMSRELI RNVYNSFYKL RDRAERIASR
     AIDNAADLLI FGKELSALGS DTTPLPSWAA LHLSTWGSLK QALKGLSVEF ALLADRAAQQ
     GKKEENDVVE KLNLFLDLLQ SYKDLCERHE KGVLHKHQRA LHKYGLMKRQ MMSAAHGREP
     ESVEQLESRI VEQENVIQTM ELRNYFSLYC LHQETQLVHV YLPLTSHILG AFVNSQIQGH
     KEMSKVWNDL KPKLSCLFAG PHSVLTPPRS PQEDGVCPH
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024