SNX14_HUMAN
ID SNX14_HUMAN Reviewed; 946 AA.
AC Q9Y5W7; B4DI55; Q4VBR3; Q5TCF9; Q5TCG0; Q6NUI7; Q6PI37; Q9BSD1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Sorting nexin-14;
GN Name=SNX14;
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Corpus callosum;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 37-946 (ISOFORM 4).
RC TISSUE=Placenta, and Testis;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 8-946 (ISOFORM 2).
RA Hong W.;
RT "The complete coding region of SNX14.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 573-946.
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 [7]
RP INVOLVEMENT IN SCAR20.
RX PubMed=25439728; DOI=10.1016/j.ajhg.2014.10.007;
RA Thomas A.C., Williams H., Seto-Salvia N., Bacchelli C., Jenkins D.,
RA O'Sullivan M., Mengrelis K., Ishida M., Ocaka L., Chanudet E., James C.,
RA Lescai F., Anderson G., Morrogh D., Ryten M., Duncan A.J., Pai Y.J.,
RA Saraiva J.M., Ramos F., Farren B., Saunders D., Vernay B., Gissen P.,
RA Straatmaan-Iwanowska A., Baas F., Wood N.W., Hersheson J., Houlden H.,
RA Hurst J., Scott R., Bitner-Glindzicz M., Moore G.E., Sousa S.B.,
RA Stanier P.;
RT "Mutations in SNX14 cause a distinctive autosomal-recessive cerebellar
RT ataxia and intellectual disability syndrome.";
RL Am. J. Hum. Genet. 95:611-621(2014).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHOINOSITIDE-BINDING, TISSUE
RP SPECIFICITY, AND INVOLVEMENT IN SCAR20.
RX PubMed=25848753; DOI=10.1038/ng.3256;
RA Akizu N., Cantagrel V., Zaki M.S., Al-Gazali L., Wang X., Rosti R.O.,
RA Dikoglu E., Gelot A.B., Rosti B., Vaux K.K., Scott E.M., Silhavy J.L.,
RA Schroth J., Copeland B., Schaffer A.E., Gordts P.L., Esko J.D.,
RA Buschman M.D., Field S.J., Napolitano G., Abdel-Salam G.M., Ozgul R.K.,
RA Sagiroglu M.S., Azam M., Ismail S., Aglan M., Selim L., Mahmoud I.G.,
RA Abdel-Hadi S., Badawy A.E., Sadek A.A., Mojahedi F., Kayserili H.,
RA Masri A., Bastaki L., Temtamy S., Mueller U., Desguerre I., Casanova J.L.,
RA Dursun A., Gunel M., Gabriel S.B., de Lonlay P., Gleeson J.G.;
RT "Biallelic mutations in SNX14 cause a syndromic form of cerebellar atrophy
RT and lysosome-autophagosome dysfunction.";
RL Nat. Genet. 47:528-534(2015).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 558-702.
RA Vollmar M., Kiyani W., Shrestha L., Goubin S., Krojer T., Pike A.C.W.,
RA Carpenter E., Quigley A., Mckenzie A., Burgess-Brown N., Von Delft F.,
RA Arrowsmith C.H., Bountra C., Edwards A., Yue W.W.;
RT "Crystal structure of the phox-homology domain of human sorting nexin 14.";
RL Submitted (MAR-2013) to the PDB data bank.
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 561-686.
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).
RN [12]
RP VARIANT SCAR20 153-TYR--MET-946 DEL.
RX PubMed=26443249;
RA Jazayeri R., Hu H., Fattahi Z., Musante L., Abedini S.S., Hosseini M.,
RA Wienker T.F., Ropers H.H., Najmabadi H., Kahrizi K.;
RT "Exome Sequencing and Linkage Analysis Identified Novel Candidate Genes in
RT Recessive Intellectual Disability Associated with Ataxia.";
RL Arch. Iran. Med. 18:670-682(2015).
CC -!- FUNCTION: Plays a role in maintaining normal neuronal excitability and
CC synaptic transmission. May be involved in several stages of
CC intracellular trafficking (By similarity). Required for autophagosome
CC clearance, possibly by mediating the fusion of lysosomes with
CC autophagosomes (Probable). Binds phosphatidylinositol 3,5-bisphosphate
CC (PtdIns(3,5)P2), a key component of late endosomes/lysosomes
CC (PubMed:25848753). Does not bind phosphatidylinositol 3-phosphate
CC (PtdIns(3P)) (PubMed:25848753, PubMed:25148684).
CC {ECO:0000250|UniProtKB:Q8BHY8, ECO:0000269|PubMed:25148684,
CC ECO:0000269|PubMed:25848753, ECO:0000305|PubMed:25848753}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:25848753};
CC Multi-pass membrane protein {ECO:0000305}. Late endosome membrane
CC {ECO:0000269|PubMed:25848753}; Multi-pass membrane protein
CC {ECO:0000305}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q8BHY8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9Y5W7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y5W7-2; Sequence=VSP_037776, VSP_037777;
CC Name=3;
CC IsoId=Q9Y5W7-3; Sequence=VSP_037775;
CC Name=4;
CC IsoId=Q9Y5W7-4; Sequence=VSP_037777;
CC -!- TISSUE SPECIFICITY: Widely expressed both in fetal and adult tissues.
CC {ECO:0000269|PubMed:25848753}.
CC -!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 20 (SCAR20)
CC [MIM:616354]: A form of spinocerebellar ataxia, a clinically and
CC genetically heterogeneous group of cerebellar disorders due to
CC degeneration of the cerebellum with variable involvement of the
CC brainstem and spinal cord. SCAR20 is characterized by cerebellar
CC atrophy, ataxia, coarsened facial features, severely delayed
CC psychomotor development with poor or absent speech, and intellectual
CC disability. {ECO:0000269|PubMed:25439728, ECO:0000269|PubMed:25848753,
CC ECO:0000269|PubMed:26443249}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AK295417; BAG58367.1; -; mRNA.
DR EMBL; AL136082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL589666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48631.1; -; Genomic_DNA.
DR EMBL; BC005110; AAH05110.2; -; mRNA.
DR EMBL; BC046520; AAH46520.1; -; mRNA.
DR EMBL; BC068589; AAH68589.1; -; mRNA.
DR EMBL; BC095419; AAH95419.1; -; mRNA.
DR EMBL; AY044865; AAK97796.1; -; mRNA.
DR EMBL; AF121863; AAD27836.1; -; mRNA.
DR CCDS; CCDS5003.1; -. [Q9Y5W7-2]
DR CCDS; CCDS5004.1; -. [Q9Y5W7-1]
DR CCDS; CCDS75490.1; -. [Q9Y5W7-4]
DR CCDS; CCDS78163.1; -. [Q9Y5W7-3]
DR RefSeq; NP_001284543.1; NM_001297614.2. [Q9Y5W7-4]
DR RefSeq; NP_001291408.1; NM_001304479.1. [Q9Y5W7-3]
DR RefSeq; NP_065201.1; NM_020468.5. [Q9Y5W7-2]
DR RefSeq; NP_722523.1; NM_153816.5. [Q9Y5W7-1]
DR PDB; 4BGJ; X-ray; 2.55 A; A=558-702.
DR PDB; 4PQO; X-ray; 2.55 A; A=561-686.
DR PDB; 4PQP; X-ray; 3.00 A; A/B/C/D=561-686.
DR PDBsum; 4BGJ; -.
DR PDBsum; 4PQO; -.
DR PDBsum; 4PQP; -.
DR AlphaFoldDB; Q9Y5W7; -.
DR SMR; Q9Y5W7; -.
DR BioGRID; 121463; 80.
DR IntAct; Q9Y5W7; 20.
DR MINT; Q9Y5W7; -.
DR STRING; 9606.ENSP00000313121; -.
DR GlyGen; Q9Y5W7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y5W7; -.
DR PhosphoSitePlus; Q9Y5W7; -.
DR BioMuta; SNX14; -.
DR DMDM; 254763401; -.
DR EPD; Q9Y5W7; -.
DR jPOST; Q9Y5W7; -.
DR MassIVE; Q9Y5W7; -.
DR MaxQB; Q9Y5W7; -.
DR PaxDb; Q9Y5W7; -.
DR PeptideAtlas; Q9Y5W7; -.
DR PRIDE; Q9Y5W7; -.
DR ProteomicsDB; 86518; -. [Q9Y5W7-1]
DR ProteomicsDB; 86519; -. [Q9Y5W7-2]
DR ProteomicsDB; 86520; -. [Q9Y5W7-3]
DR ProteomicsDB; 86521; -. [Q9Y5W7-4]
DR Antibodypedia; 3006; 81 antibodies from 17 providers.
DR DNASU; 57231; -.
DR Ensembl; ENST00000314673.8; ENSP00000313121.3; ENSG00000135317.14. [Q9Y5W7-1]
DR Ensembl; ENST00000346348.7; ENSP00000257769.3; ENSG00000135317.14. [Q9Y5W7-2]
DR Ensembl; ENST00000369627.6; ENSP00000358641.2; ENSG00000135317.14. [Q9Y5W7-4]
DR Ensembl; ENST00000505648.5; ENSP00000427380.1; ENSG00000135317.14. [Q9Y5W7-3]
DR GeneID; 57231; -.
DR KEGG; hsa:57231; -.
DR MANE-Select; ENST00000314673.8; ENSP00000313121.3; NM_153816.6; NP_722523.1.
DR UCSC; uc003pkr.4; human. [Q9Y5W7-1]
DR CTD; 57231; -.
DR DisGeNET; 57231; -.
DR GeneCards; SNX14; -.
DR HGNC; HGNC:14977; SNX14.
DR HPA; ENSG00000135317; Low tissue specificity.
DR MalaCards; SNX14; -.
DR MIM; 616105; gene.
DR MIM; 616354; phenotype.
DR neXtProt; NX_Q9Y5W7; -.
DR OpenTargets; ENSG00000135317; -.
DR Orphanet; 397709; Intellectual disability-coarse face-macrocephaly-cerebellar hypotrophy syndrome.
DR PharmGKB; PA129840867; -.
DR VEuPathDB; HostDB:ENSG00000135317; -.
DR eggNOG; KOG2101; Eukaryota.
DR GeneTree; ENSGT00950000182856; -.
DR HOGENOM; CLU_014115_0_0_1; -.
DR InParanoid; Q9Y5W7; -.
DR OMA; VKARQKX; -.
DR OrthoDB; 257375at2759; -.
DR PhylomeDB; Q9Y5W7; -.
DR TreeFam; TF324055; -.
DR PathwayCommons; Q9Y5W7; -.
DR SignaLink; Q9Y5W7; -.
DR BioGRID-ORCS; 57231; 31 hits in 1081 CRISPR screens.
DR ChiTaRS; SNX14; human.
DR GenomeRNAi; 57231; -.
DR Pharos; Q9Y5W7; Tbio.
DR PRO; PR:Q9Y5W7; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9Y5W7; protein.
DR Bgee; ENSG00000135317; Expressed in left testis and 175 other tissues.
DR ExpressionAtlas; Q9Y5W7; baseline and differential.
DR Genevisible; Q9Y5W7; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd06877; PX_SNX14; 1.
DR CDD; cd08722; RGS_SNX14; 1.
DR Gene3D; 1.10.167.10; -; 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; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR037436; SNX14_PX.
DR InterPro; IPR037892; SNX14_RGS.
DR InterPro; IPR013937; Sorting_nexin_C.
DR Pfam; PF08628; Nexin_C; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF02194; PXA; 1.
DR Pfam; PF00615; RGS; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00313; PXA; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS51207; PXA; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Disease variant;
KW Endosome; Intellectual disability; Lysosome; Membrane; Neurodegeneration;
KW Phosphoprotein; Protein transport; Reference proteome;
KW Spinocerebellar ataxia; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..946
FT /note="Sorting nexin-14"
FT /id="PRO_0000213861"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 130..304
FT /note="PXA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147,
FT ECO:0000255|PROSITE-ProRule:PRU00553"
FT DOMAIN 336..468
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 570..690
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037775"
FT VAR_SEQ 140..183
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5"
FT /id="VSP_037776"
FT VAR_SEQ 483..491
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5"
FT /id="VSP_037777"
FT VARIANT 153..946
FT /note="Missing (in SCAR20)"
FT /evidence="ECO:0000269|PubMed:26443249"
FT /id="VAR_083399"
FT CONFLICT 60
FT /note="A -> V (in Ref. 4; AAH68589)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="P -> R (in Ref. 4; AAH68589)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="F -> I (in Ref. 4; AAH46520)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="L -> P (in Ref. 4; AAH46520)"
FT /evidence="ECO:0000305"
FT CONFLICT 696
FT /note="I -> L (in Ref. 4; AAH95419)"
FT /evidence="ECO:0000305"
FT CONFLICT 882
FT /note="Y -> C (in Ref. 4; AAH46520)"
FT /evidence="ECO:0000305"
FT HELIX 562..564
FT /evidence="ECO:0007829|PDB:4BGJ"
FT STRAND 565..575
FT /evidence="ECO:0007829|PDB:4BGJ"
FT STRAND 589..598
FT /evidence="ECO:0007829|PDB:4BGJ"
FT STRAND 609..615
FT /evidence="ECO:0007829|PDB:4BGJ"
FT HELIX 617..631
FT /evidence="ECO:0007829|PDB:4BGJ"
FT STRAND 635..637
FT /evidence="ECO:0007829|PDB:4PQP"
FT HELIX 650..668
FT /evidence="ECO:0007829|PDB:4BGJ"
FT HELIX 671..673
FT /evidence="ECO:0007829|PDB:4BGJ"
FT HELIX 677..682
FT /evidence="ECO:0007829|PDB:4BGJ"
SQ SEQUENCE 946 AA; 110182 MW; CDC5D0A918BC16B9 CRC64;
MVPWVRTMGQ KLKQRLRLDV GREICRQYPL FCFLLLCLSA ASLLLNRYIH ILMIFWSFVA
GVVTFYCSLG PDSLLPNIFF TIKYKPKQLG LQELFPQGHS CAVCGKVKCK RHRPSLLLEN
YQPWLDLKIS SKVDASLSEV LELVLENFVY PWYRDVTDDE SFVDELRITL RFFASVLIRR
IHKVDIPSII TKKLLKAAMK HIEVIVKARQ KVKNTEFLQQ AALEEYGPEL HVALRSRRDE
LHYLRKLTEL LFPYILPPKA TDCRSLTLLI REILSGSVFL PSLDFLADPD TVNHLLIIFI
DDSPPEKATE PASPLVPFLQ KFAEPRNKKP SVLKLELKQI REQQDLLFRF MNFLKQEGAV
HVLQFCLTVE EFNDRILRPE LSNDEMLSLH EELQKIYKTY CLDESIDKIR FDPFIVEEIQ
RIAEGPYIDV VKLQTMRCLF EAYEHVLSLL ENVFTPMFCH SDEYFRQLLR GAESPTRNSK
LNRGSLSLDD FRNTQKRGES FGISRIGSKI KGVFKSTTME GAMLPNYGVA EGEDDFIEEG
IVVMEDDSPV EAVSTPNTPR NLAAWKISIP YVDFFEDPSS ERKEKKERIP VFCIDVERND
RRAVGHEPEH WSVYRRYLEF YVLESKLTEF HGAFPDAQLP SKRIIGPKNY EFLKSKREEF
QEYLQKLLQH PELSNSQLLA DFLSPNGGET QFLDKILPDV NLGKIIKSVP GKLMKEKGQH
LEPFIMNFIN SCESPKPKPS RPELTILSPT SENNKKLFND LFKNNANRAE NTERKQNQNY
FMEVMTVEGV YDYLMYVGRV VFQVPDWLHH LLMGTRILFK NTLEMYTDYY LQCKLEQLFQ
EHRLVSLITL LRDAIFCENT EPRSLQDKQK GAKQTFEEMM NYIPDLLVKC IGEETKYESI
RLLFDGLQQP VLNKQLTYVL LDIVIQELFP ELNKVQKEVT SVTSWM
