SNX22_HUMAN
ID SNX22_HUMAN Reviewed; 193 AA.
AC Q96L94; Q8WUS9; Q9H844;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Sorting nexin-22;
GN Name=SNX22;
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).
RA Hong W.;
RT "A novel member (SNX22) of the sorting nexin family.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [5]
RP STRUCTURE BY NMR OF 2-120, DOMAIN, SUBCELLULAR LOCATION, AND
RP PHOSPHATIDYLINOSITOL 3-PHOSPHATE BINDING.
RX PubMed=17400918; DOI=10.1110/ps.072752407;
RA Song J., Zhao K.Q., Newman C.L., Vinarov D.A., Markley J.L.;
RT "Solution structure of human sorting nexin 22.";
RL Protein Sci. 16:807-814(2007).
CC -!- FUNCTION: May be involved in several stages of intracellular
CC trafficking (By similarity). Interacts with membranes containing
CC phosphatidylinositol 3-phosphate (PtdIns(3P)). {ECO:0000250}.
CC -!- INTERACTION:
CC Q96L94-2; Q92997: DVL3; NbExp=3; IntAct=EBI-12310305, EBI-739789;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96L94-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96L94-2; Sequence=VSP_056595;
CC -!- DOMAIN: The PX domain mediates specific binding to membranes enriched
CC in phosphatidylinositol 3-phosphate (PtdIns(P3)).
CC {ECO:0000269|PubMed:17400918}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {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; AY044653; AAK98767.1; -; mRNA.
DR EMBL; AK024014; BAB14776.1; -; mRNA.
DR EMBL; AC100840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019655; AAH19655.1; -; mRNA.
DR CCDS; CCDS10190.1; -. [Q96L94-1]
DR RefSeq; NP_079074.2; NM_024798.2. [Q96L94-1]
DR PDB; 2ETT; NMR; -; A=2-120.
DR PDBsum; 2ETT; -.
DR AlphaFoldDB; Q96L94; -.
DR BMRB; Q96L94; -.
DR SMR; Q96L94; -.
DR BioGRID; 122945; 11.
DR IntAct; Q96L94; 8.
DR MINT; Q96L94; -.
DR STRING; 9606.ENSP00000323435; -.
DR iPTMnet; Q96L94; -.
DR PhosphoSitePlus; Q96L94; -.
DR BioMuta; SNX22; -.
DR DMDM; 20140142; -.
DR MassIVE; Q96L94; -.
DR MaxQB; Q96L94; -.
DR PaxDb; Q96L94; -.
DR PeptideAtlas; Q96L94; -.
DR PRIDE; Q96L94; -.
DR ProteomicsDB; 74706; -.
DR ProteomicsDB; 77170; -. [Q96L94-1]
DR Antibodypedia; 51656; 49 antibodies from 12 providers.
DR DNASU; 79856; -.
DR Ensembl; ENST00000325881.9; ENSP00000323435.4; ENSG00000157734.14. [Q96L94-1]
DR Ensembl; ENST00000558466.5; ENSP00000452692.1; ENSG00000157734.14. [Q96L94-2]
DR GeneID; 79856; -.
DR KEGG; hsa:79856; -.
DR MANE-Select; ENST00000325881.9; ENSP00000323435.4; NM_024798.3; NP_079074.2.
DR UCSC; uc002anc.1; human. [Q96L94-1]
DR CTD; 79856; -.
DR DisGeNET; 79856; -.
DR GeneCards; SNX22; -.
DR HGNC; HGNC:16315; SNX22.
DR HPA; ENSG00000157734; Tissue enhanced (brain, thyroid gland).
DR MalaCards; SNX22; -.
DR neXtProt; NX_Q96L94; -.
DR OpenTargets; ENSG00000157734; -.
DR PharmGKB; PA134897329; -.
DR VEuPathDB; HostDB:ENSG00000157734; -.
DR eggNOG; KOG2101; Eukaryota.
DR GeneTree; ENSGT00390000001280; -.
DR HOGENOM; CLU_117250_0_0_1; -.
DR InParanoid; Q96L94; -.
DR OMA; LTFHCDP; -.
DR PhylomeDB; Q96L94; -.
DR TreeFam; TF332414; -.
DR PathwayCommons; Q96L94; -.
DR SignaLink; Q96L94; -.
DR BioGRID-ORCS; 79856; 32 hits in 1076 CRISPR screens.
DR ChiTaRS; SNX22; human.
DR EvolutionaryTrace; Q96L94; -.
DR GenomeRNAi; 79856; -.
DR Pharos; Q96L94; Tdark.
DR PRO; PR:Q96L94; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q96L94; protein.
DR Bgee; ENSG00000157734; Expressed in right lobe of thyroid gland and 154 other tissues.
DR ExpressionAtlas; Q96L94; baseline and differential.
DR Genevisible; Q96L94; HS.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IBA:GO_Central.
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 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; Cytoplasmic vesicle; Lipid-binding;
KW Membrane; Protein transport; Reference proteome; Transport.
FT CHAIN 1..193
FT /note="Sorting nexin-22"
FT /id="PRO_0000213871"
FT DOMAIN 1..118
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT BINDING 45
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT BINDING 66
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT BINDING 79
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT VAR_SEQ 121..193
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056595"
FT CONFLICT 191
FT /note="P -> L (in Ref. 2; BAB14776)"
FT /evidence="ECO:0000305"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:2ETT"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:2ETT"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:2ETT"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:2ETT"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:2ETT"
FT HELIX 76..93
FT /evidence="ECO:0007829|PDB:2ETT"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:2ETT"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:2ETT"
SQ SEQUENCE 193 AA; 22068 MW; B57D8F8B737F429E CRC64;
MLEVHIPSVG PEAEGPRQSP EKSHMVFRVE VLCSGRRHTV PRRYSEFHAL HKRIKKLYKV
PDFPSKRLPN WRTRGLEQRR QGLEAYIQGI LYLNQEVPKE LLEFLRLRHF PTDPKASNWG
TLREFLPGDS SSQQHQRPVL SFHVDPYVCN PSPESLPNVV VNGVLQGLYS FSISPDKAQP
KAACHPAPLP PMP
