SPE39_HUMAN
ID SPE39_HUMAN Reviewed; 493 AA.
AC Q9H9C1; B4DPI6; O95434; Q9H7E1; Q9H9I9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Spermatogenesis-defective protein 39 homolog;
DE Short=hSPE-39;
DE AltName: Full=VPS33B-interacting protein in apical-basolateral polarity regulator;
DE AltName: Full=VPS33B-interacting protein in polarity and apical restriction;
GN Name=VIPAS39; Synonyms=C14orf133, SPE39, VIPAR;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney;
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=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-132, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP FUNCTION, INTERACTION WITH VPS33A; VPS33B AND HOPS COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19109425; DOI=10.1091/mbc.e08-07-0728;
RA Zhu G.D., Salazar G., Zlatic S.A., Fiza B., Doucette M.M., Heilman C.J.,
RA Levey A.I., Faundez V., L'hernault S.W.;
RT "SPE-39 family proteins interact with the HOPS complex and function in
RT lysosomal delivery.";
RL Mol. Biol. Cell 20:1223-1240(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP FUNCTION, INTERACTION WITH RAB11A AND VPS33B, SUBCELLULAR LOCATION, AND
RP INVOLVEMENT IN ARCS1.
RX PubMed=20190753; DOI=10.1038/ng.538;
RA Cullinane A.R., Straatman-Iwanowska A., Zaucker A., Wakabayashi Y.,
RA Bruce C.K., Luo G., Rahman F., Gurakan F., Utine E., Ozkan T.B.,
RA Denecke J., Vukovic J., Di Rocco M., Mandel H., Cangul H., Matthews R.P.,
RA Thomas S.G., Rappoport J.Z., Arias I.M., Wolburg H., Knisely A.S.,
RA Kelly D.A., Muller F., Maher E.R., Gissen P.;
RT "Mutations in VIPAR cause an arthrogryposis, renal dysfunction and
RT cholestasis syndrome phenotype with defects in epithelial polarization.";
RL Nat. Genet. 42:303-312(2010).
RN [8]
RP GENE NOMENCLATURE.
RX PubMed=21350494; DOI=10.1038/ng0311-176;
RA L'Hernault S.W., Faundez V.;
RT "On the endosomal function and gene nomenclature of human SPE-39.";
RL Nat. Genet. 43:176-176(2011).
RN [9]
RP INTERACTION WITH VPS33B.
RX PubMed=23918659; DOI=10.1093/hmg/ddt378;
RA Tornieri K., Zlatic S.A., Mullin A.P., Werner E., Harrison R.,
RA L'hernault S.W., Faundez V.;
RT "Vps33b pathogenic mutations preferentially affect VIPAS39/SPE-39-positive
RT endosomes.";
RL Hum. Mol. Genet. 22:5215-5228(2013).
RN [10]
RP SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF LEU-213.
RX PubMed=22753090; DOI=10.1002/humu.22155;
RA Smith H., Galmes R., Gogolina E., Straatman-Iwanowska A., Reay K.,
RA Banushi B., Bruce C.K., Cullinane A.R., Romero R., Chang R., Ackermann O.,
RA Baumann C., Cangul H., Cakmak Celik F., Aygun C., Coward R.,
RA Dionisi-Vici C., Sibbles B., Inward C., Kim C.A., Klumperman J.,
RA Knisely A.S., Watson S.P., Gissen P.;
RT "Associations among genotype, clinical phenotype, and intracellular
RT localization of trafficking proteins in ARC syndrome.";
RL Hum. Mutat. 33:1656-1664(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21; SER-121; SER-124 AND
RP SER-130, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP INTERACTION WITH VPS33B.
RX PubMed=23901104; DOI=10.1073/pnas.1307074110;
RA Graham S.C., Wartosch L., Gray S.R., Scourfield E.J., Deane J.E.,
RA Luzio J.P., Owen D.J.;
RT "Structural basis of Vps33A recruitment to the human HOPS complex by
RT Vps16.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:13345-13350(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, 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).
CC -!- FUNCTION: Proposed to be involved in endosomal maturation implicating
CC in part VPS33B. In epithelial cells, the VPS33B:VIPAS39 complex may
CC play a role in the apical RAB11A-dependent recycling pathway and in the
CC maintenance of the apical-basolateral polarity (PubMed:20190753). May
CC play a role in lysosomal trafficking, probably via association with the
CC core HOPS complex in a discrete population of endosomes; the functions
CC seems to be independent of VPS33B (PubMed:19109425). May play a role in
CC vesicular trafficking during spermatogenesis (By similarity). May be
CC involved in direct or indirect transcriptional regulation of E-cadherin
CC (By similarity). {ECO:0000250|UniProtKB:Q23288,
CC ECO:0000269|PubMed:19109425, ECO:0000269|PubMed:20190753}.
CC -!- SUBUNIT: Interacts with VPS33B (PubMed:19109425, PubMed:23901104).
CC Associates with the homotypic fusion and vacuole protein sorting (HOPS)
CC complex; impaired by VPS33B (PubMed:19109425, PubMed:23918659,
CC PubMed:22753090). A possible interaction with VPS33A is reported
CC conflictingly (PubMed:19109425, PubMed:23901104). Interacts with RAB11A
CC (PubMed:20190753). {ECO:0000269|PubMed:19109425,
CC ECO:0000269|PubMed:20190753, ECO:0000269|PubMed:22753090}.
CC -!- INTERACTION:
CC Q9H9C1; Q9H267: VPS33B; NbExp=39; IntAct=EBI-749080, EBI-749072;
CC Q9H9C1; P49754: VPS41; NbExp=4; IntAct=EBI-749080, EBI-2130459;
CC Q9H9C1; Q91W86: Vps11; Xeno; NbExp=3; IntAct=EBI-749080, EBI-2527812;
CC Q9H9C1; Q920Q4: Vps16; Xeno; NbExp=4; IntAct=EBI-749080, EBI-775797;
CC Q9H9C1; Q8R307: Vps18; Xeno; NbExp=5; IntAct=EBI-749080, EBI-2527788;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle
CC {ECO:0000250}. Early endosome {ECO:0000269|PubMed:19109425}. Recycling
CC endosome {ECO:0000269|PubMed:19109425, ECO:0000269|PubMed:22753090}.
CC Late endosome {ECO:0000269|PubMed:19109425}. Note=Colocalizes in
CC clusters with VPS33B at cytoplasmic organelles (PubMed:19109425).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H9C1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H9C1-2; Sequence=VSP_043055;
CC -!- DISEASE: Arthrogryposis, renal dysfunction and cholestasis syndrome 2
CC (ARCS2) [MIM:613404]: A multisystem disorder, characterized by
CC neurogenic arthrogryposis multiplex congenita, renal tubular
CC dysfunction and neonatal cholestasis with bile duct hypoplasia and low
CC gamma glutamyl transpeptidase activity. Platelet dysfunction is common.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry. In liver, CEACAM5 and ABCB11 are mislocalized and E-
CC cadherin expression is decreased.
CC -!- SIMILARITY: Belongs to the SPE39 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD09624.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB14951.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK024661; BAB14951.1; ALT_INIT; mRNA.
DR EMBL; AK022769; BAB14237.1; -; mRNA.
DR EMBL; AK022925; BAB14310.1; -; mRNA.
DR EMBL; AK298354; BAG60598.1; -; mRNA.
DR EMBL; AF111168; AAD09624.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC015054; AAH15054.1; -; mRNA.
DR CCDS; CCDS53905.1; -. [Q9H9C1-2]
DR CCDS; CCDS9862.1; -. [Q9H9C1-1]
DR RefSeq; NP_001180243.1; NM_001193314.1. [Q9H9C1-1]
DR RefSeq; NP_001180244.1; NM_001193315.1. [Q9H9C1-1]
DR RefSeq; NP_001180245.1; NM_001193316.1. [Q9H9C1-2]
DR RefSeq; NP_001180246.1; NM_001193317.1. [Q9H9C1-1]
DR RefSeq; NP_071350.2; NM_022067.3. [Q9H9C1-1]
DR AlphaFoldDB; Q9H9C1; -.
DR SMR; Q9H9C1; -.
DR BioGRID; 121974; 52.
DR ComplexPortal; CPX-6241; CHEVI tethering complex.
DR CORUM; Q9H9C1; -.
DR IntAct; Q9H9C1; 20.
DR MINT; Q9H9C1; -.
DR STRING; 9606.ENSP00000452181; -.
DR iPTMnet; Q9H9C1; -.
DR PhosphoSitePlus; Q9H9C1; -.
DR BioMuta; VIPAS39; -.
DR DMDM; 41016926; -.
DR EPD; Q9H9C1; -.
DR jPOST; Q9H9C1; -.
DR MassIVE; Q9H9C1; -.
DR MaxQB; Q9H9C1; -.
DR PaxDb; Q9H9C1; -.
DR PeptideAtlas; Q9H9C1; -.
DR PRIDE; Q9H9C1; -.
DR Antibodypedia; 26048; 126 antibodies from 22 providers.
DR DNASU; 63894; -.
DR Ensembl; ENST00000327028.8; ENSP00000313098.5; ENSG00000151445.16. [Q9H9C1-2]
DR Ensembl; ENST00000343765.6; ENSP00000339122.2; ENSG00000151445.16. [Q9H9C1-1]
DR Ensembl; ENST00000448935.6; ENSP00000404815.2; ENSG00000151445.16. [Q9H9C1-2]
DR Ensembl; ENST00000553888.5; ENSP00000452181.1; ENSG00000151445.16. [Q9H9C1-1]
DR Ensembl; ENST00000557658.6; ENSP00000452191.1; ENSG00000151445.16. [Q9H9C1-1]
DR GeneID; 63894; -.
DR KEGG; hsa:63894; -.
DR MANE-Select; ENST00000557658.6; ENSP00000452191.1; NM_001193315.2; NP_001180244.1.
DR UCSC; uc001xtt.3; human. [Q9H9C1-1]
DR CTD; 63894; -.
DR DisGeNET; 63894; -.
DR GeneCards; VIPAS39; -.
DR HGNC; HGNC:20347; VIPAS39.
DR HPA; ENSG00000151445; Low tissue specificity.
DR MalaCards; VIPAS39; -.
DR MIM; 613401; gene.
DR MIM; 613404; phenotype.
DR neXtProt; NX_Q9H9C1; -.
DR OpenTargets; ENSG00000151445; -.
DR Orphanet; 2697; Arthrogryposis-renal dysfunction-cholestasis syndrome.
DR PharmGKB; PA165479332; -.
DR VEuPathDB; HostDB:ENSG00000151445; -.
DR eggNOG; KOG4677; Eukaryota.
DR GeneTree; ENSGT00390000013955; -.
DR HOGENOM; CLU_029487_0_0_1; -.
DR InParanoid; Q9H9C1; -.
DR PhylomeDB; Q9H9C1; -.
DR TreeFam; TF319640; -.
DR PathwayCommons; Q9H9C1; -.
DR SignaLink; Q9H9C1; -.
DR SIGNOR; Q9H9C1; -.
DR BioGRID-ORCS; 63894; 9 hits in 1075 CRISPR screens.
DR GenomeRNAi; 63894; -.
DR Pharos; Q9H9C1; Tbio.
DR PRO; PR:Q9H9C1; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9H9C1; protein.
DR Bgee; ENSG00000151445; Expressed in cortical plate and 192 other tissues.
DR ExpressionAtlas; Q9H9C1; baseline and differential.
DR Genevisible; Q9H9C1; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0099023; C:vesicle tethering complex; IPI:ComplexPortal.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0032963; P:collagen metabolic process; IMP:MGI.
DR GO; GO:0008333; P:endosome to lysosome transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0046907; P:intracellular transport; IC:ComplexPortal.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; IMP:MGI.
DR GO; GO:0090385; P:phagosome-lysosome fusion; IC:ComplexPortal.
DR GO; GO:0043687; P:post-translational protein modification; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007034; P:vacuolar transport; IBA:GO_Central.
DR Gene3D; 1.10.150.780; -; 1.
DR InterPro; IPR040057; Spe-39.
DR InterPro; IPR006925; Vps16_C.
DR InterPro; IPR038132; Vps16_C_sf.
DR PANTHER; PTHR13364; PTHR13364; 1.
DR Pfam; PF04840; Vps16_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Differentiation;
KW Endosome; Phosphoprotein; Protein transport; Reference proteome;
KW Spermatogenesis; Transcription; Transcription regulation; Transport.
FT CHAIN 1..493
FT /note="Spermatogenesis-defective protein 39 homolog"
FT /id="PRO_0000089935"
FT REGION 68..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 117
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGQ1"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 132
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 67..115
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043055"
FT MUTAGEN 213
FT /note="L->P: Disrupts endodsomal colocalization with
FT VPS33B."
FT /evidence="ECO:0000269|PubMed:22753090"
FT CONFLICT 280
FT /note="L -> S (in Ref. 1; BAB14237)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 57005 MW; CF05C38EB922D192 CRC64;
MNRTKGDEEE YWNSSKFKAF TFDDEDDELS QLKESKRAVN SLRDFVDDDD DDDLERVSWS
GEPVGSISWS IRETAGNSGS THEGREQLKS RNSFSSYAQL PKPTSTYSLS SFFRGRTRPG
SFQSLSDALS DTPAKSYAPE LGRPKGEYRD YSNDWSPSDT VRRLRKGKVC SLERFRSLQD
KLQLLEEAVS MHDGNVITAV LIFLKRTLSK EILFRELEVR QVALRHLIHF LKEIGDQKLL
LDLFRFLDRT EELALSHYRE HLNIQDPDKR KEFLKTCVGL PFSAEDSAHI QDHYTLLERQ
IIIEANDRHL ESAGQTEIFR KHPRKASILN MPLVTTLFYS CFYHYTEAEG TFSSPVNLKK
TFKIPDKQYV LTALAARAKL RAWNDVDALF TTKNWLGYTK KRAPIGFHRV VEILHKNNAP
VQILQEYVNL VEDVDTKLNL ATKFKCHDVV IDTYRDLKDR QQLLAYRSKV DKGSAEEEKI
DALLSSSQIR WKN
