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Database: UniProt
Entry: B5RHZ3_DANRE
LinkDB: B5RHZ3_DANRE
Original site: B5RHZ3_DANRE 
ID   B5RHZ3_DANRE            Unreviewed;       551 AA.
AC   B5RHZ3; A0A8M1NI80;
DT   04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=Sorting nexin {ECO:0000256|PIRNR:PIRNR027744};
GN   Name=snx33 {ECO:0000313|EMBL:AAI69193.1,
GN   ECO:0000313|Ensembl:ENSDARP00000006712,
GN   ECO:0000313|RefSeq:NP_001116327.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-041111-209};
GN   Synonyms=im:7144315 {ECO:0000313|EMBL:AAI69193.1,
GN   ECO:0000313|RefSeq:NP_001116327.1}, sh3px3
GN   {ECO:0000313|EMBL:AAI69193.1, ECO:0000313|RefSeq:NP_001116327.1},
GN   zgc:113233 {ECO:0000313|RefSeq:NP_001116327.1}, zgc:195632
GN   {ECO:0000313|RefSeq:NP_001116327.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI69193.1};
RN   [1] {ECO:0000313|RefSeq:NP_001116327.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001116327.1};
RX   PubMed=22213104;
RA   Xu L., Yin W., Xia J., Peng M., Li S., Lin S., Pei D., Shu X.;
RT   "An antiapoptotic role of sorting nexin 7 is required for liver development
RT   in zebrafish.";
RL   Hepatology 55:1985-1993(2012).
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000006712}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000006712};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSDARP00000006712, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000006712};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [4] {ECO:0000313|RefSeq:NP_001116327.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001116327.1};
RX   PubMed=26469318;
RA   Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA   Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA   Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA   Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA   Reith W., Hertzano R.;
RT   "RFX transcription factors are essential for hearing in mice.";
RL   Nat. Commun. 6:8549-8549(2015).
RN   [5] {ECO:0000313|EMBL:AAI69193.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Adult ovary {ECO:0000313|EMBL:AAI69193.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|RefSeq:NP_001116327.1}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001116327.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC       {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004180}.
CC   -!- SIMILARITY: Belongs to the sorting nexin family.
CC       {ECO:0000256|ARBA:ARBA00010883, ECO:0000256|PIRNR:PIRNR027744}.
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DR   EMBL; CR354425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC169193; AAI69193.1; -; mRNA.
DR   RefSeq; NP_001116327.1; NM_001122855.2.
DR   STRING; 7955.ENSDARP00000006712; -.
DR   PaxDb; 7955-ENSDARP00000006712; -.
DR   Ensembl; ENSDART00000009971.9; ENSDARP00000006712.7; ENSDARG00000014954.10.
DR   GeneID; 100001421; -.
DR   KEGG; dre:100001421; -.
DR   AGR; ZFIN:ZDB-GENE-041111-209; -.
DR   CTD; 257364; -.
DR   ZFIN; ZDB-GENE-041111-209; snx33.
DR   eggNOG; KOG2528; Eukaryota.
DR   HOGENOM; CLU_021494_1_0_1; -.
DR   OMA; NINSPVY; -.
DR   OrthoDB; 5401713at2759; -.
DR   TreeFam; TF314082; -.
DR   Proteomes; UP000000437; Chromosome 25.
DR   Bgee; ENSDARG00000014954; Expressed in swim bladder and 19 other cell types or tissues.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR   GO; GO:0036089; P:cleavage furrow formation; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0000281; P:mitotic cytokinesis; IEA:InterPro.
DR   GO; GO:0097320; P:plasma membrane tubulation; IBA:GO_Central.
DR   CDD; cd07669; BAR_SNX33; 1.
DR   CDD; cd11896; SH3_SNX33; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR037427; SNX33_BAR.
DR   InterPro; IPR014536; Snx9_fam.
DR   InterPro; IPR019497; Sorting_nexin_WASP-bd-dom.
DR   PANTHER; PTHR45827; SORTING NEXIN; 1.
DR   PANTHER; PTHR45827:SF3; SORTING NEXIN-33; 1.
DR   Pfam; PF10456; BAR_3_WASP_bdg; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   PIRSF; PIRSF027744; Snx9; 1.
DR   SMART; SM00312; PX; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50195; PX; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW   ECO:0000256|PIRNR:PIRNR027744};
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR027744};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:B5RHZ3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022927}.
FT   DOMAIN          1..61
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          207..317
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   REGION          65..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..109
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         243
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR027744-1"
FT   BINDING         245
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR027744-1"
FT   BINDING         283
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR027744-1"
SQ   SEQUENCE   551 AA;  63980 MW;  3927105F54A1FD63 CRC64;
     MSLRAKALYT FQSENKEEIN IQENEELVIF DENSVDGWLQ GENSRGERGL FPASYVHIIR
     SRSGSNLTDQ SFSSPGSSPG KDLSYIHTPS TTLPSDDDDD WDDWDETSTV VEDDDHRRGA
     NGHSQNQYSN PNVHYRSKPY MDRQDSMSSN RKGSMVGRNL NRFSSFVRSG VEAFILGDVP
     MMAKIAESYS IEMGPRGPQW MDNPRPFSCS IEDPTKQTKF KGIKTYISYR VTPSHTGRPV
     YRRYKHFDWL YNRLLHKFTV ISVPHLPEKQ ATGRFEEDFI EKRKRRLILW MDHMTSHPVL
     SQYEGFEHFL MCGDDKQWKL GKRRAEKDEM VGAHFMLTFQ IPNEHQDLQD VEERIDSFKS
     FAKKMDDSVM QLTNVASELV RKHLGGFRKE FQRLGNGFQS ISQSFLLDPP YSSDALSNAI
     SHTGRTYENI GEMFADQPKN DLFQMLDKLS LYQGLLSNFP DIIHLQKGAF AKVKESQRMS
     DEGKMDQGEA DGIRKRCRTV GFALQAEMNH FHQRREVDFK EMMQAYLRQQ IAFYQRVGQQ
     LERTLRMYDN L
//
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