SNX19_MOUSE
ID SNX19_MOUSE Reviewed; 997 AA.
AC Q6P4T1; Q3TQ83; Q80U53;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Sorting nexin-19;
GN Name=Snx19 {ECO:0000312|MGI:MGI:1921581};
GN Synonyms=Kiaa0254 {ECO:0000312|EMBL:BAC65513.1};
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 {ECO:0000312|EMBL:AAH63262.1};
RN [1] {ECO:0000312|EMBL:BAC65513.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:BAC65513.1};
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2] {ECO:0000312|Ensembl:ENSMUSP00000131895, ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000131895,
RC ECO:0000312|Proteomes:UP000000589};
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH63262.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH63262.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-348.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE37501.1};
RC TISSUE=Head {ECO:0000312|EMBL:BAE37501.1};
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, 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).
RN [6]
RP FUNCTION.
RX PubMed=24843546; DOI=10.1111/j.2040-1124.2011.00138.x;
RA Harashima S., Horiuchi T., Wang Y., Notkins A.L., Seino Y., Inagaki N.;
RT "Sorting nexin 19 regulates the number of dense core vesicles in pancreatic
RT beta-cells.";
RL J. Diabetes Investig. 3:52-61(2012).
RN [7] {ECO:0007744|PDB:4P2I, ECO:0007744|PDB:4P2J}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 528-664, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF ARG-587 AND ARG-634, AND BINDING SITES.
RX PubMed=25148684; DOI=10.1074/jbc.m114.595959;
RA Mas C., Norwood S.J., Bugarcic A., Kinna G., Leneva N., Kovtun O., Ghai R.,
RA Ona Yanez L.E., Davis J.L., Teasdale R.D., Collins B.M.;
RT "Structural basis for different phosphoinositide specificities of the PX
RT domains of sorting nexins regulating G-protein signaling.";
RL J. Biol. Chem. 289:28554-28568(2014).
CC -!- FUNCTION: Plays a role in intracellular vesicle trafficking and
CC exocytosis (PubMed:24843546). May play a role in maintaining insulin-
CC containing dense core vesicles in pancreatic beta-cells and in
CC preventing their degradation. May play a role in insulin secretion
CC (PubMed:24843546). Interacts with membranes containing
CC phosphatidylinositol 3-phosphate (PtdIns(3P)) (PubMed:25148684).
CC {ECO:0000269|PubMed:24843546, ECO:0000269|PubMed:25148684}.
CC -!- SUBUNIT: Interacts with PTPRN. {ECO:0000250|UniProtKB:Q92543}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000305|PubMed:25148684}; Peripheral membrane protein
CC {ECO:0000269|PubMed:25148684}; Cytoplasmic side
CC {ECO:0000269|PubMed:25148684}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:25148684}; Peripheral membrane protein
CC {ECO:0000269|PubMed:25148684}; Cytoplasmic side
CC {ECO:0000269|PubMed:25148684}.
CC -!- DOMAIN: The PX domain mediates specific binding to membranes enriched
CC in phosphatidylinositol 3-phosphate (PtdIns(P3)).
CC {ECO:0000269|PubMed:25148684}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65513.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122231; BAC65513.1; ALT_INIT; mRNA.
DR EMBL; AC160339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU024910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC063262; AAH63262.1; -; mRNA.
DR EMBL; AK163810; BAE37501.1; -; mRNA.
DR CCDS; CCDS22944.1; -.
DR RefSeq; NP_083150.1; NM_028874.2.
DR PDB; 4P2I; X-ray; 1.90 A; A/B=528-664.
DR PDB; 4P2J; X-ray; 2.40 A; A/B=528-664.
DR PDBsum; 4P2I; -.
DR PDBsum; 4P2J; -.
DR AlphaFoldDB; Q6P4T1; -.
DR SMR; Q6P4T1; -.
DR STRING; 10090.ENSMUSP00000131895; -.
DR iPTMnet; Q6P4T1; -.
DR PhosphoSitePlus; Q6P4T1; -.
DR EPD; Q6P4T1; -.
DR MaxQB; Q6P4T1; -.
DR PaxDb; Q6P4T1; -.
DR PRIDE; Q6P4T1; -.
DR ProteomicsDB; 261468; -.
DR Antibodypedia; 2996; 97 antibodies from 27 providers.
DR Ensembl; ENSMUST00000164099; ENSMUSP00000131895; ENSMUSG00000031993.
DR GeneID; 102607; -.
DR KEGG; mmu:102607; -.
DR UCSC; uc009oqy.1; mouse.
DR CTD; 399979; -.
DR MGI; MGI:1921581; Snx19.
DR VEuPathDB; HostDB:ENSMUSG00000031993; -.
DR eggNOG; ENOG502QQBH; Eukaryota.
DR GeneTree; ENSGT00950000182856; -.
DR HOGENOM; CLU_012033_0_0_1; -.
DR InParanoid; Q6P4T1; -.
DR OMA; PDWIHLI; -.
DR OrthoDB; 1342782at2759; -.
DR PhylomeDB; Q6P4T1; -.
DR TreeFam; TF324055; -.
DR BioGRID-ORCS; 102607; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Snx19; mouse.
DR PRO; PR:Q6P4T1; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q6P4T1; protein.
DR Bgee; ENSMUSG00000031993; Expressed in saccule of membranous labyrinth and 243 other tissues.
DR ExpressionAtlas; Q6P4T1; baseline and differential.
DR Genevisible; Q6P4T1; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0002062; P:chondrocyte differentiation; IMP:MGI.
DR GO; GO:1990502; P:dense core granule maturation; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0030073; P:insulin secretion; IMP:MGI.
DR CDD; cd06893; PX_SNX19; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR003114; Phox_assoc.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR034908; SNX19.
DR InterPro; IPR037909; SNX19_PX.
DR InterPro; IPR013937; Sorting_nexin_C.
DR PANTHER; PTHR22775:SF31; PTHR22775:SF31; 1.
DR Pfam; PF08628; Nexin_C; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF02194; PXA; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00313; PXA; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS51207; PXA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Endosome; Exocytosis; Lipid-binding;
KW Membrane; Protein transport; Reference proteome; Transport.
FT CHAIN 1..997
FT /note="Sorting nexin-19"
FT /id="PRO_0000434599"
FT DOMAIN 95..273
FT /note="PXA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00553"
FT DOMAIN 538..668
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 313..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 587
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:25148684"
FT BINDING 634
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:25148684"
FT MUTAGEN 587
FT /note="R->A: Abolishes location on endosome membranes."
FT /evidence="ECO:0000269|PubMed:25148684"
FT MUTAGEN 587
FT /note="R->Q: Abolishes interaction with membranes enriched
FT in phosphatidylinositol 3-phosphate."
FT /evidence="ECO:0000269|PubMed:25148684"
FT MUTAGEN 634
FT /note="R->K: Abolishes interaction with membranes enriched
FT in phosphatidylinositol 3-phosphate. Abolishes location on
FT endosome membranes."
FT /evidence="ECO:0000269|PubMed:25148684"
FT STRAND 535..549
FT /evidence="ECO:0007829|PDB:4P2I"
FT STRAND 551..568
FT /evidence="ECO:0007829|PDB:4P2I"
FT STRAND 578..586
FT /evidence="ECO:0007829|PDB:4P2I"
FT HELIX 588..599
FT /evidence="ECO:0007829|PDB:4P2I"
FT HELIX 602..605
FT /evidence="ECO:0007829|PDB:4P2I"
FT HELIX 606..608
FT /evidence="ECO:0007829|PDB:4P2I"
FT HELIX 628..646
FT /evidence="ECO:0007829|PDB:4P2I"
FT HELIX 649..652
FT /evidence="ECO:0007829|PDB:4P2I"
FT HELIX 655..660
FT /evidence="ECO:0007829|PDB:4P2I"
SQ SEQUENCE 997 AA; 109808 MW; AA8241D6F7BCCC71 CRC64;
MKAQTVSPTQ GTISESSYVH SNLWSSRKLM IVGVLVGWLL VIHLLVNMWL LILLCASLVA
LGGWLGSTAI LGASGQLHLE RFITITTCPP CPEAERQLEQ EINRTIQMII RDFVLSWYRS
VSHEPAFEAE MEAAMKGLVQ ELRRRMSIVD SHALTQRVLT LCGCHLQSYI QAKEATAKEQ
SCPVQPSQLW DAYCQVTAPH PAMSCPTTEV TYARGIVNLI LKELVPKPHL ETRTGRHVVV
EVITCNVILP LISKLSDPDW IHLILVSIFS KYRHDAAQGT KPPCSSSVLE QPSVPTSLPL
IVEVESLPVG KASSPATAPV HLTSSEPAPS PEIEEGHEAV EGDLPGMLEE KKVGNSSSHF
LQPDIRGPLF LCEDSELESP LSELSKETIL LMTPGNFLSD RIQDALCALD DSGALEPKDG
EGSECMEGAE AEEAPGTDTE TGMLVSVLNC PEIQIDTADK EVEQGDDTSL TALLEEPEKP
CPLRPSCLDK DLASGVCSLE PAMPPVPLSS SPPGPLSSAT FSFESLSSPD GPVVIQNLRI
TGTITAREHS GTGFHPYTLY TVKYETVLNG ENSSGLQQLA YHTVNRRYRE FLNLQTRLEE
KPDLRKFIKN VKGPKKLFPD LPFGNMDSDR VEARKSLLES FLKQLCAIPE IGNSEEVQEF
LALNTDARIA FVKKPFMVSR IDKMVVSAIV DTLKTAFPRS EPQSPTEELS EAENESKPQT
EGKKASKSRL RFSSSKIAPA LSIAEAQDKI LYCLQEGNSE SEVLSMSGME SFIEKQTKLL
RIQPAEVPDK DPQQVPKEYV DSGLLDKAVV AQELNKSGPG TETELADTAF DLILLLLMEQ
WKWLCTESMQ KFLHIIFGTL VQRWLEVQVA NLTCPQRWAQ YLHLLRESIW PGGVLPKFPR
PGRTQAQKAA TEKQALQSLM DLLPDFLVEI LGVNKCRLSW SLVLESFQQP LINRHLIYCL
GDIILELLDL SASVEECAPA TSASDSPGSL KKMAVST
