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SNX21_MOUSE
ID   SNX21_MOUSE             Reviewed;         363 AA.
AC   Q3UR97;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Sorting nexin-21 {ECO:0000305};
GN   Name=Snx21 {ECO:0000312|MGI:MGI:1917729};
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=Embryo;
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] {ECO:0000312|Ensembl:ENSMUSP00000054137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000054137};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3] {ECO:0007744|PDB:4YMR}
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 230-363, SUBUNIT, SUBCELLULAR
RP   LOCATION, DOMAIN, AND MUTAGENESIS OF ARG-161.
RX   PubMed=25882846; DOI=10.1074/jbc.m115.650598;
RA   Clairfeuille T., Norwood S.J., Qi X., Teasdale R.D., Collins B.M.;
RT   "Structure and membrane binding properties of the endosomal
RT   tetratricopeptide repeat (TPR) domain-containing sorting nexins SNX20 and
RT   SNX21.";
RL   J. Biol. Chem. 290:14504-14517(2015).
CC   -!- FUNCTION: Binds to membranes enriched in phosphatidylinositol 3-
CC       phosphate (PtdIns(P3)) and phosphatidylinositol 4,5-bisphosphate
CC       (PubMed:25882846). May be involved in several stages of intracellular
CC       trafficking. {ECO:0000269|PubMed:25882846, ECO:0000305}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25882846}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC       {ECO:0000305|PubMed:25882846}; Peripheral membrane protein
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Early endosome membrane
CC       {ECO:0000269|PubMed:25882846}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:25882846}; Cytoplasmic side
CC       {ECO:0000269|PubMed:25882846}.
CC   -!- DOMAIN: The PX domain mediates specific binding to membranes enriched
CC       in phosphatidylinositol 3-phosphate (PtdIns(P3)).
CC       {ECO:0000269|PubMed:25882846}.
CC   -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR   EMBL; AL591127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK141663; BAE24791.1; -; mRNA.
DR   CCDS; CCDS38328.1; -.
DR   RefSeq; NP_598685.2; NM_133924.3.
DR   PDB; 4YMR; X-ray; 2.40 A; A/B=230-363.
DR   PDBsum; 4YMR; -.
DR   AlphaFoldDB; Q3UR97; -.
DR   SMR; Q3UR97; -.
DR   STRING; 10090.ENSMUSP00000054137; -.
DR   iPTMnet; Q3UR97; -.
DR   PhosphoSitePlus; Q3UR97; -.
DR   MaxQB; Q3UR97; -.
DR   PaxDb; Q3UR97; -.
DR   PeptideAtlas; Q3UR97; -.
DR   PRIDE; Q3UR97; -.
DR   ProteomicsDB; 261541; -.
DR   Antibodypedia; 27775; 82 antibodies from 17 providers.
DR   DNASU; 101113; -.
DR   Ensembl; ENSMUST00000056181; ENSMUSP00000054137; ENSMUSG00000050373.
DR   GeneID; 101113; -.
DR   KEGG; mmu:101113; -.
DR   UCSC; uc008nwc.1; mouse.
DR   CTD; 90203; -.
DR   MGI; MGI:1917729; Snx21.
DR   VEuPathDB; HostDB:ENSMUSG00000050373; -.
DR   eggNOG; KOG2101; Eukaryota.
DR   GeneTree; ENSGT00530000063759; -.
DR   HOGENOM; CLU_059132_0_0_1; -.
DR   InParanoid; Q3UR97; -.
DR   OMA; EAQEHCD; -.
DR   OrthoDB; 1322681at2759; -.
DR   PhylomeDB; Q3UR97; -.
DR   TreeFam; TF326807; -.
DR   BioGRID-ORCS; 101113; 1 hit in 71 CRISPR screens.
DR   ChiTaRS; Snx21; mouse.
DR   PRO; PR:Q3UR97; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q3UR97; protein.
DR   Bgee; ENSMUSG00000050373; Expressed in hindlimb stylopod muscle and 200 other tissues.
DR   ExpressionAtlas; Q3UR97; baseline and differential.
DR   Genevisible; Q3UR97; MM.
DR   GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR   GO; GO:1901981; F:phosphatidylinositol phosphate binding; IBA:GO_Central.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1520.10; -; 1.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR039937; SNX20/SNX21.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR20939; PTHR20939; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF64268; SSF64268; 1.
DR   PROSITE; PS50195; PX; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasmic vesicle; Endosome; Lipid-binding; Membrane;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..363
FT                   /note="Sorting nexin-21"
FT                   /id="PRO_0000434600"
FT   DOMAIN          119..236
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   REGION          1..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..73
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         161
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:0000305|PubMed:25882846"
FT   BINDING         163
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|UniProtKB:Q96L94"
FT   BINDING         188
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|UniProtKB:Q96L94"
FT   BINDING         202
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|UniProtKB:Q6P4T1"
FT   MUTAGEN         161
FT                   /note="R->Q: Abolishes location on endosome membranes.
FT                   Abolishes binding to membranes enriched in
FT                   phosphatidylinositol 3-phosphate. No significant effect on
FT                   binding to membranes enriched in phosphatidylinositol 4,5-
FT                   bisphosphate."
FT                   /evidence="ECO:0000269|PubMed:25882846"
FT   HELIX           231..243
FT                   /evidence="ECO:0007829|PDB:4YMR"
FT   HELIX           246..262
FT                   /evidence="ECO:0007829|PDB:4YMR"
FT   STRAND          263..265
FT                   /evidence="ECO:0007829|PDB:4YMR"
FT   HELIX           271..285
FT                   /evidence="ECO:0007829|PDB:4YMR"
FT   HELIX           289..304
FT                   /evidence="ECO:0007829|PDB:4YMR"
FT   HELIX           312..325
FT                   /evidence="ECO:0007829|PDB:4YMR"
FT   HELIX           331..341
FT                   /evidence="ECO:0007829|PDB:4YMR"
FT   TURN            342..344
FT                   /evidence="ECO:0007829|PDB:4YMR"
FT   HELIX           353..359
FT                   /evidence="ECO:0007829|PDB:4YMR"
SQ   SEQUENCE   363 AA;  40308 MW;  076DEBEA6EA7AC4F CRC64;
     MASRLLHRLR HALASDGPGE AAAGPEAEQF PESSELEDDD AEGLSSRLSG TLSFTSAEDD
     PDDEDEDDEA GLDSPPSGDG ASGEDAERSP PPDGQRSSQL LARQLQDFWK KSRNTLVPQR
     LLFEVTSANV VKDPPSKYVL YTLAVMGPGP PDRQPAQISR RYSDFERLHR NLQRQFRGPM
     SAISFPRKRL RRNFTAETIA RRSRAFEQFL GHLQAVPELR QAPDLQDFFV LPELRRAQSL
     TCTGLYREAL ALWANAWQLQ TQLGTPSGPD RPLLTLAGLA VCHQELEDPG EARACSEKAL
     QLLGDKRPHP FLAPFLEAHV RLSWRLGLDK RQSEAQLQAL QEAGLTSTPP PSLKELLIKE
     VLD
 
 
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