SNX11_HUMAN
ID SNX11_HUMAN Reviewed; 270 AA.
AC Q9Y5W9; B3KRL6; B4DPY5; D3DTV0; Q53YC0; Q9H885;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Sorting nexin-11;
GN Name=SNX11;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11485546; DOI=10.1042/0264-6021:3580007;
RA Teasdale R.D., Loci D., Houghton F., Karlsson L., Gleeson P.A.;
RT "A large family of endosome-localized proteins related to sorting nexin
RT 1.";
RL Biochem. J. 358:7-16(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, Testis, and Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney, and Skin;
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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 7-170, FUNCTION, SUBUNIT,
RP LIPID-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-59 AND
RP 135-ILE--VAL-139.
RX PubMed=23615901; DOI=10.1074/jbc.m112.449306;
RA Xu J., Xu T., Wu B., Ye Y., You X., Shu X., Pei D., Liu J.;
RT "Structure of Sorting Nexin 11 (SNX11) reveals a novel extended PX Domain
RT (PXe Domain) critical for the inhibition of Sorting Nexin 10 (SNX10)
RT induced vacuolation.";
RL J. Biol. Chem. 288:16598-16605(2013).
CC -!- FUNCTION: Phosphoinositide-binding protein involved in protein sorting
CC and membrane trafficking in endosomes. {ECO:0000269|PubMed:23615901}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23615901}.
CC -!- INTERACTION:
CC Q9Y5W9; Q15041: ARL6IP1; NbExp=6; IntAct=EBI-10329449, EBI-714543;
CC Q9Y5W9; Q3KP22-3: MAJIN; NbExp=3; IntAct=EBI-10329449, EBI-18015780;
CC Q9Y5W9; Q8N987: NECAB1; NbExp=3; IntAct=EBI-10329449, EBI-11956853;
CC Q9Y5W9; Q9UI14: RABAC1; NbExp=6; IntAct=EBI-10329449, EBI-712367;
CC Q9Y5W9; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-10329449, EBI-14065960;
CC Q9Y5W9; Q9NS64: RPRM; NbExp=3; IntAct=EBI-10329449, EBI-1052363;
CC Q9Y5W9; Q8NB12: SMYD1; NbExp=3; IntAct=EBI-10329449, EBI-8463848;
CC Q9Y5W9; Q9NRG4: SMYD2; NbExp=3; IntAct=EBI-10329449, EBI-1055671;
CC Q9Y5W9; O95070: YIF1A; NbExp=3; IntAct=EBI-10329449, EBI-2799703;
CC Q9Y5W9; O75800: ZMYND10; NbExp=3; IntAct=EBI-10329449, EBI-747061;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endosome
CC {ECO:0000269|PubMed:23615901}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y5W9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y5W9-2; Sequence=VSP_056594;
CC -!- DOMAIN: The PX domain mediates interaction with membranes enriched in
CC phosphatidylinositol 3-phosphate. {ECO:0000269|PubMed:23615901}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD27834.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF121861; AAD27834.1; ALT_INIT; mRNA.
DR EMBL; BT006723; AAP35369.1; -; mRNA.
DR EMBL; AK023932; BAB14732.1; -; mRNA.
DR EMBL; AK091852; BAG52428.1; -; mRNA.
DR EMBL; AK298551; BAG60747.1; -; mRNA.
DR EMBL; AK316374; BAH14745.1; -; mRNA.
DR EMBL; AC006468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94754.1; -; Genomic_DNA.
DR EMBL; BC000768; AAH00768.1; -; mRNA.
DR EMBL; BC103721; AAI03722.1; -; mRNA.
DR CCDS; CCDS11526.1; -. [Q9Y5W9-1]
DR CCDS; CCDS82152.1; -. [Q9Y5W9-2]
DR RefSeq; NP_001317249.1; NM_001330320.1. [Q9Y5W9-2]
DR RefSeq; NP_037455.2; NM_013323.2. [Q9Y5W9-1]
DR RefSeq; NP_689450.1; NM_152244.1. [Q9Y5W9-1]
DR RefSeq; XP_005257317.1; XM_005257260.3. [Q9Y5W9-1]
DR RefSeq; XP_005257319.1; XM_005257262.3. [Q9Y5W9-2]
DR RefSeq; XP_011522999.1; XM_011524697.2. [Q9Y5W9-1]
DR PDB; 4IKB; X-ray; 1.78 A; A/B=7-142.
DR PDB; 4IKD; X-ray; 1.60 A; A=7-170.
DR PDB; 6KOI; X-ray; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=7-158.
DR PDB; 6KOJ; X-ray; 2.14 A; A/B=7-142.
DR PDB; 6KOK; X-ray; 2.00 A; A/B=7-139.
DR PDBsum; 4IKB; -.
DR PDBsum; 4IKD; -.
DR PDBsum; 6KOI; -.
DR PDBsum; 6KOJ; -.
DR PDBsum; 6KOK; -.
DR AlphaFoldDB; Q9Y5W9; -.
DR SMR; Q9Y5W9; -.
DR BioGRID; 118960; 33.
DR IntAct; Q9Y5W9; 25.
DR STRING; 9606.ENSP00000377059; -.
DR iPTMnet; Q9Y5W9; -.
DR MetOSite; Q9Y5W9; -.
DR PhosphoSitePlus; Q9Y5W9; -.
DR SwissPalm; Q9Y5W9; -.
DR BioMuta; SNX11; -.
DR DMDM; 14916716; -.
DR EPD; Q9Y5W9; -.
DR jPOST; Q9Y5W9; -.
DR MassIVE; Q9Y5W9; -.
DR MaxQB; Q9Y5W9; -.
DR PaxDb; Q9Y5W9; -.
DR PeptideAtlas; Q9Y5W9; -.
DR PRIDE; Q9Y5W9; -.
DR ProteomicsDB; 86524; -. [Q9Y5W9-1]
DR Antibodypedia; 30244; 137 antibodies from 21 providers.
DR DNASU; 29916; -.
DR Ensembl; ENST00000359238.7; ENSP00000352175.2; ENSG00000002919.15. [Q9Y5W9-1]
DR Ensembl; ENST00000393405.6; ENSP00000377059.2; ENSG00000002919.15. [Q9Y5W9-1]
DR Ensembl; ENST00000580219.5; ENSP00000462188.1; ENSG00000002919.15. [Q9Y5W9-2]
DR Ensembl; ENST00000582104.5; ENSP00000463948.1; ENSG00000002919.15. [Q9Y5W9-2]
DR GeneID; 29916; -.
DR KEGG; hsa:29916; -.
DR MANE-Select; ENST00000359238.7; ENSP00000352175.2; NM_013323.3; NP_037455.2.
DR UCSC; uc002inf.2; human. [Q9Y5W9-1]
DR CTD; 29916; -.
DR DisGeNET; 29916; -.
DR GeneCards; SNX11; -.
DR HGNC; HGNC:14975; SNX11.
DR HPA; ENSG00000002919; Low tissue specificity.
DR MIM; 614906; gene.
DR neXtProt; NX_Q9Y5W9; -.
DR OpenTargets; ENSG00000002919; -.
DR PharmGKB; PA37951; -.
DR VEuPathDB; HostDB:ENSG00000002919; -.
DR eggNOG; KOG2527; Eukaryota.
DR GeneTree; ENSGT00940000160113; -.
DR InParanoid; Q9Y5W9; -.
DR OMA; DQPNSCC; -.
DR OrthoDB; 1407986at2759; -.
DR PhylomeDB; Q9Y5W9; -.
DR TreeFam; TF332117; -.
DR PathwayCommons; Q9Y5W9; -.
DR SignaLink; Q9Y5W9; -.
DR BioGRID-ORCS; 29916; 13 hits in 1078 CRISPR screens.
DR ChiTaRS; SNX11; human.
DR GenomeRNAi; 29916; -.
DR Pharos; Q9Y5W9; Tdark.
DR PRO; PR:Q9Y5W9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9Y5W9; protein.
DR Bgee; ENSG00000002919; Expressed in oral epithelium and 181 other tissues.
DR ExpressionAtlas; Q9Y5W9; baseline and differential.
DR Genevisible; Q9Y5W9; HS.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016050; P:vesicle organization; IMP:UniProtKB.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR043544; SNX10/11.
DR PANTHER; PTHR46209; PTHR46209; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Endosome; Lipid-binding; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..270
FT /note="Sorting nexin-11"
FT /id="PRO_0000213856"
FT DOMAIN 16..132
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 135..139
FT /note="Important for membrane trafficking"
FT REGION 168..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT BINDING 85
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 99
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 VAR_SEQ 1..14
FT /note="MGFWCRMSENQEQE -> MVCREQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056594"
FT MUTAGEN 59
FT /note="R->A: Abolishes lipid-binding."
FT /evidence="ECO:0000269|PubMed:23615901"
FT MUTAGEN 135..139
FT /note="IEACV->AAAAA: Impairs function in membrane
FT trafficking."
FT /evidence="ECO:0000269|PubMed:23615901"
FT STRAND 17..28
FT /evidence="ECO:0007829|PDB:4IKD"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:4IKD"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4IKD"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:4IKD"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:4IKD"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:6KOI"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4IKB"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:4IKD"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:4IKD"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:4IKD"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:4IKD"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:4IKD"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:4IKD"
FT HELIX 147..156
FT /evidence="ECO:0007829|PDB:4IKD"
SQ SEQUENCE 270 AA; 30433 MW; E6839B7415F1724F CRC64;
MGFWCRMSEN QEQEEVITVR VQDPRVQNEG SWNSYVDYKI FLHTNSKAFT AKTSCVRRRY
REFVWLRKQL QRNAGLVPVP ELPGKSTFFG TSDEFIEKRR QGLQHFLEKV LQSVVLLSDS
QLHLFLQSQL SVPEIEACVQ GRSTMTVSDA ILRYAMSNCG WAQEERQSSS HLAKGDQPKS
CCFLPRSGRR SSPSPPPSEE KDHLEVWAPV VDSEVPSLES PTLPPLSSPL CCDFGRPKEG
TSTLQSVRRA VGGDHAVPLD PGQLETVLEK
