VP13C_HUMAN
ID VP13C_HUMAN Reviewed; 3753 AA.
AC Q709C8; Q6ISR4; Q702P2; Q702P3; Q709C9; Q9NXN8; Q9P2C6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Intermembrane lipid transfer protein VPS13C {ECO:0000303|PubMed:30093493};
DE AltName: Full=Vacuolar protein sorting-associated protein 13C {ECO:0000305};
GN Name=VPS13C {ECO:0000312|EMBL:AAH69387.1};
GN Synonyms=KIAA1421 {ECO:0000312|EMBL:BAA92659.1};
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] {ECO:0000305, ECO:0000312|EMBL:CAE75583.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Lymphoblast {ECO:0000269|PubMed:15498460};
RX PubMed=15498460; DOI=10.1016/j.ygeno.2004.04.012;
RA Velayos-Baeza A., Vettori A., Copley R.R., Dobson-Stone C., Monaco A.P.;
RT "Analysis of the human VPS13 gene family.";
RL Genomics 84:536-549(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAA92659.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1439 (ISOFORMS 1/2), AND
RP VARIANT LYS-974.
RC TISSUE=Brain {ECO:0000312|EMBL:BAA92659.1};
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAA90972.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3305-3753 (ISOFORMS 1/3).
RC TISSUE=Colon {ECO:0000312|EMBL:BAA90972.1};
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAH69387.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3305-3753 (ISOFORMS 1/3).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-614; SER-619; THR-624 AND
RP SER-737, AND IDENTIFICATION BY 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3538, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-737; SER-842 AND SER-3641,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2473, 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 [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-3526, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN PARK23, AND VARIANT PARK23
RP ARG-1389.
RX PubMed=26942284; DOI=10.1016/j.ajhg.2016.01.014;
RG French Parkinson's Disease Genetics Study (PDG);
RG International Parkinson's Disease Genomics Consortium (IPDGC);
RG International Parkinson's Disease Genomics Consortium IPDGC;
RA Lesage S., Drouet V., Majounie E., Deramecourt V., Jacoupy M., Nicolas A.,
RA Cormier-Dequaire F., Hassoun S.M., Pujol C., Ciura S., Erpapazoglou Z.,
RA Usenko T., Maurage C.A., Sahbatou M., Liebau S., Ding J., Bilgic B.,
RA Emre M., Erginel-Unaltuna N., Guven G., Tison F., Tranchant C.,
RA Vidailhet M., Corvol J.C., Krack P., Leutenegger A.L., Nalls M.A.,
RA Hernandez D.G., Heutink P., Gibbs J.R., Hardy J., Wood N.W., Gasser T.,
RA Durr A., Deleuze J.F., Tazir M., Destee A., Lohmann E., Kabashi E.,
RA Singleton A., Corti O., Brice A.;
RT "Loss of mitochondrial morphology, transmembrane potential, and respiration
RT function in autosomal-recessive parkinsonism causes mitochondrial
RT dysfunction and increases PINK1/Parkin-dependent mitophagy.";
RL Am. J. Hum. Genet. 98:500-513(2016).
RN [14]
RP VARIANT PHE-2872.
RX PubMed=25787250; DOI=10.1073/pnas.1503696112;
RA Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W.,
RA Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D., Stalberg P.,
RA Akerstroem G., Westin G., Hellman P., Carling T., Bjoerklund P.,
RA Lifton R.P.;
RT "Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in
RT insulin-producing adenomas.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015).
RN [15]
RP SUBCELLULAR LOCATION, DOMAIN FFAT MOTIF, AND MUTAGENESIS OF
RP 878-TYR-PHE-879.
RX PubMed=30093493; DOI=10.1083/jcb.201807019;
RA Kumar N., Leonzino M., Hancock-Cerutti W., Horenkamp F.A., Li P.,
RA Lees J.A., Wheeler H., Reinisch K.M., De Camilli P.;
RT "VPS13A and VPS13C are lipid transport proteins differentially localized at
RT ER contact sites.";
RL J. Cell Biol. 217:3625-3639(2018).
CC -!- FUNCTION: Mediates the transfer of lipids between membranes at
CC organelle contact sites (By similarity). Necessary for proper
CC mitochondrial function and maintenance of mitochondrial transmembrane
CC potential (PubMed:26942284). Involved in the regulation of PINK1/PRKN-
CC mediated mitophagy in response to mitochondrial depolarization
CC (PubMed:26942284). {ECO:0000250|UniProtKB:Q07878,
CC ECO:0000269|PubMed:26942284}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:26942284}. Lipid droplet
CC {ECO:0000269|PubMed:30093493}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:30093493}. Lysosome membrane
CC {ECO:0000269|PubMed:30093493}. Late endosome membrane
CC {ECO:0000269|PubMed:30093493}. Note=May localize to endoplasmic
CC reticulum-endolysosome contact sites. {ECO:0000269|PubMed:30093493}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:15498460}; Synonyms=2A
CC {ECO:0000269|PubMed:15498460};
CC IsoId=Q709C8-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15498460}; Synonyms=2B
CC {ECO:0000269|PubMed:15498460};
CC IsoId=Q709C8-2; Sequence=VSP_052244, VSP_052245;
CC Name=3 {ECO:0000269|PubMed:15498460}; Synonyms=1A
CC {ECO:0000269|PubMed:15498460};
CC IsoId=Q709C8-3; Sequence=VSP_052243;
CC Name=4 {ECO:0000269|PubMed:15498460}; Synonyms=1B
CC {ECO:0000269|PubMed:15498460};
CC IsoId=Q709C8-4; Sequence=VSP_052243, VSP_052244, VSP_052245;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15498460}.
CC -!- DOMAIN: The FFAT motif is required for localization to the endoplasmic
CC reticulum. {ECO:0000269|PubMed:30093493}.
CC -!- DISEASE: Parkinson disease 23, autosomal recessive, early onset
CC (PARK23) [MIM:616840]: An autosomal recessive, early-onset form of
CC Parkinson disease, a complex neurodegenerative disorder characterized
CC by bradykinesia, resting tremor, muscular rigidity and postural
CC instability, as well as by a clinically significant response to
CC treatment with levodopa. The pathology involves the loss of
CC dopaminergic neurons in the substantia nigra and the presence of Lewy
CC bodies (intraneuronal accumulations of aggregated proteins), in
CC surviving neurons in various areas of the brain.
CC {ECO:0000269|PubMed:26942284}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the VPS13 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA90972.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA92659.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ608770; CAE75582.1; -; mRNA.
DR EMBL; AJ608771; CAE75583.1; -; mRNA.
DR EMBL; AJ626860; CAF25187.1; -; mRNA.
DR EMBL; AJ626861; CAF25188.1; -; mRNA.
DR EMBL; AB037842; BAA92659.1; ALT_INIT; mRNA.
DR EMBL; AK000143; BAA90972.1; ALT_INIT; mRNA.
DR EMBL; BC069387; AAH69387.1; -; mRNA.
DR CCDS; CCDS10180.1; -. [Q709C8-3]
DR CCDS; CCDS32257.1; -. [Q709C8-1]
DR CCDS; CCDS45272.1; -. [Q709C8-2]
DR CCDS; CCDS58367.1; -. [Q709C8-4]
DR RefSeq; NP_001018098.1; NM_001018088.2. [Q709C8-2]
DR RefSeq; NP_060154.3; NM_017684.4. [Q709C8-3]
DR RefSeq; NP_060550.2; NM_018080.3. [Q709C8-4]
DR RefSeq; NP_065872.1; NM_020821.2. [Q709C8-1]
DR BioGRID; 120186; 87.
DR ELM; Q709C8; -.
DR IntAct; Q709C8; 23.
DR MINT; Q709C8; -.
DR STRING; 9606.ENSP00000261517; -.
DR CarbonylDB; Q709C8; -.
DR iPTMnet; Q709C8; -.
DR MetOSite; Q709C8; -.
DR PhosphoSitePlus; Q709C8; -.
DR BioMuta; VPS13C; -.
DR DMDM; 74712594; -.
DR EPD; Q709C8; -.
DR jPOST; Q709C8; -.
DR MassIVE; Q709C8; -.
DR MaxQB; Q709C8; -.
DR PaxDb; Q709C8; -.
DR PeptideAtlas; Q709C8; -.
DR PRIDE; Q709C8; -.
DR ProteomicsDB; 68512; -. [Q709C8-1]
DR ProteomicsDB; 68513; -. [Q709C8-2]
DR ProteomicsDB; 68514; -. [Q709C8-3]
DR ProteomicsDB; 68515; -. [Q709C8-4]
DR Antibodypedia; 50681; 13 antibodies from 8 providers.
DR DNASU; 54832; -.
DR Ensembl; ENST00000249837.7; ENSP00000249837.3; ENSG00000129003.19. [Q709C8-3]
DR Ensembl; ENST00000395898.3; ENSP00000379235.3; ENSG00000129003.19. [Q709C8-4]
DR Ensembl; ENST00000644861.2; ENSP00000493560.2; ENSG00000129003.19. [Q709C8-1]
DR Ensembl; ENST00000645819.1; ENSP00000496179.1; ENSG00000129003.19. [Q709C8-2]
DR GeneID; 54832; -.
DR KEGG; hsa:54832; -.
DR MANE-Select; ENST00000644861.2; ENSP00000493560.2; NM_020821.3; NP_065872.1.
DR UCSC; uc002agz.4; human. [Q709C8-1]
DR CTD; 54832; -.
DR DisGeNET; 54832; -.
DR GeneCards; VPS13C; -.
DR HGNC; HGNC:23594; VPS13C.
DR HPA; ENSG00000129003; Low tissue specificity.
DR MalaCards; VPS13C; -.
DR MIM; 608879; gene.
DR MIM; 616840; phenotype.
DR neXtProt; NX_Q709C8; -.
DR OpenTargets; ENSG00000129003; -.
DR Orphanet; 2828; Young-onset Parkinson disease.
DR PharmGKB; PA134990089; -.
DR VEuPathDB; HostDB:ENSG00000129003; -.
DR eggNOG; KOG1809; Eukaryota.
DR GeneTree; ENSGT00950000183083; -.
DR HOGENOM; CLU_000135_1_1_1; -.
DR InParanoid; Q709C8; -.
DR OMA; VDVRDWS; -.
DR OrthoDB; 4159at2759; -.
DR PhylomeDB; Q709C8; -.
DR TreeFam; TF300316; -.
DR PathwayCommons; Q709C8; -.
DR SignaLink; Q709C8; -.
DR BioGRID-ORCS; 54832; 8 hits in 1078 CRISPR screens.
DR ChiTaRS; VPS13C; human.
DR GenomeRNAi; 54832; -.
DR Pharos; Q709C8; Tbio.
DR PRO; PR:Q709C8; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q709C8; protein.
DR Bgee; ENSG00000129003; Expressed in calcaneal tendon and 204 other tissues.
DR ExpressionAtlas; Q709C8; baseline and differential.
DR Genevisible; Q709C8; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032127; C:dense core granule membrane; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006895; P:Golgi to endosome transport; TAS:ParkinsonsUK-UCL.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0007005; P:mitochondrion organization; IMP:ParkinsonsUK-UCL.
DR GO; GO:1905090; P:negative regulation of parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0045053; P:protein retention in Golgi apparatus; IBA:GO_Central.
DR GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR InterPro; IPR015412; Autophagy-rel_C.
DR InterPro; IPR026847; VPS13.
DR InterPro; IPR026854; VPS13-like_N.
DR InterPro; IPR031645; VPS13_C.
DR InterPro; IPR031642; VPS13_mid_rpt.
DR InterPro; IPR031646; VPS13_N2.
DR InterPro; IPR009543; VPS13_VAB.
DR PANTHER; PTHR16166; PTHR16166; 2.
DR Pfam; PF09333; ATG_C; 1.
DR Pfam; PF12624; Chorein_N; 1.
DR Pfam; PF06650; SHR-BD; 1.
DR Pfam; PF16908; VPS13; 1.
DR Pfam; PF16909; VPS13_C; 1.
DR Pfam; PF16910; VPS13_mid_rpt; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Disease variant; Endoplasmic reticulum;
KW Endosome; Lipid droplet; Lipid transport; Lysosome; Membrane; Methylation;
KW Mitochondrion; Mitochondrion outer membrane; Neurodegeneration;
KW Parkinson disease; Parkinsonism; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..3753
FT /note="Intermembrane lipid transfer protein VPS13C"
FT /id="PRO_0000262949"
FT DOMAIN 3..116
FT /note="Chorein N-terminal"
FT /evidence="ECO:0000255"
FT DOMAIN 2766..3016
FT /note="SHR-BD"
FT /evidence="ECO:0000255"
FT REGION 150..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2415..3309
FT /note="Required for late endosome/lysosome localization"
FT /evidence="ECO:0000269|PubMed:30093493"
FT REGION 3310..3753
FT /note="Required for lipid droplet localization"
FT /evidence="ECO:0000269|PubMed:30093493"
FT MOTIF 877..883
FT /note="FFAT"
FT /evidence="ECO:0000305"
FT COMPBIAS 150..164
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BX70"
FT MOD_RES 614
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 624
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 842
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 872
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BX70"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BX70"
FT MOD_RES 1979
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BX70"
FT MOD_RES 2473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 3519
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BX70"
FT MOD_RES 3526
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 3538
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 3641
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 129..171
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15498460"
FT /id="VSP_052243"
FT VAR_SEQ 3622..3627
FT /note="NHIKKL -> QELEIQE (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15498460"
FT /id="VSP_052244"
FT VAR_SEQ 3628..3753
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15498460"
FT /id="VSP_052245"
FT VARIANT 153
FT /note="R -> H (in dbSNP:rs12595158)"
FT /id="VAR_029548"
FT VARIANT 974
FT /note="R -> K (in dbSNP:rs3784634)"
FT /evidence="ECO:0000269|PubMed:10718198"
FT /id="VAR_029549"
FT VARIANT 1132
FT /note="I -> V (in dbSNP:rs3784635)"
FT /id="VAR_029550"
FT VARIANT 1302
FT /note="Y -> C (in dbSNP:rs2303405)"
FT /id="VAR_029551"
FT VARIANT 1389
FT /note="G -> R (in PARK23; dbSNP:rs369100678)"
FT /evidence="ECO:0000269|PubMed:26942284"
FT /id="VAR_076363"
FT VARIANT 1485
FT /note="T -> A (in dbSNP:rs8026956)"
FT /id="VAR_029552"
FT VARIANT 1495
FT /note="I -> V (in dbSNP:rs11629598)"
FT /id="VAR_029553"
FT VARIANT 1592
FT /note="S -> Y (in dbSNP:rs11629838)"
FT /id="VAR_029554"
FT VARIANT 2322
FT /note="V -> M (in dbSNP:rs12907567)"
FT /id="VAR_029555"
FT VARIANT 2808
FT /note="K -> R (in dbSNP:rs34060567)"
FT /id="VAR_053808"
FT VARIANT 2872
FT /note="C -> F"
FT /evidence="ECO:0000269|PubMed:25787250"
FT /id="VAR_074191"
FT VARIANT 2913
FT /note="S -> N (in dbSNP:rs10851704)"
FT /id="VAR_029556"
FT MUTAGEN 878..879
FT /note="YF->SL: Abnormal localization to the cytosol."
FT /evidence="ECO:0000269|PubMed:30093493"
SQ SEQUENCE 3753 AA; 422390 MW; 8B51A6778A89F639 CRC64;
MVLESVVADL LNRFLGDYVE NLNKSQLKLG IWGGNVALDN LQIKENALSE LDVPFKVKAG
QIDKLTLKIP WKNLYGEAVV ATLEGLYLLV VPGASIKYDA VKEEKSLQDV KQKELSRIEE
ALQKAAEKGT HSGEFIYGLE NFVYKDIKPG RKRKKHKKHF KKPFKGLDRS KDKPKEAKKD
TFVEKLATQV IKNVQVKITD IHIKYEDDVT DPKRPLSFGV TLGELSLLTA NEHWTPCILN
EADKIIYKLI RLDSLSAYWN VNCSMSYQRS REQILDQLKN EILTSGNIPP NYQYIFQPIS
ASAKLYMNPY AESELKTPKL DCNIEIQNIA IELTKPQYLS MIDLLESVDY MVRNAPYRKY
KPYLPLHTNG RRWWKYAIDS VLEVHIRRYT QMWSWSNIKK HRQLLKSYKI AYKNKLTQSK
VSEEIQKEIQ DLEKTLDVFN IILARQQAQV EVIRSGQKLR KKSADTGEKR GGWFSGLWGK
KESKKKDEES LIPETIDDLM TPEEKDKLFT AIGYSESTHN LTLPKQYVAH IMTLKLVSTS
VTIRENKNIP EILKIQIIGL GTQVSQRPGA QALKVEAKLE HWYITGLRQQ DIVPSLVASI
GDTTSSLLKI KFETNPEDSP ADQTLIVQSQ PVEVIYDAKT VNAVVEFFQS NKGLDLEQIT
SATLMKLEEI KERTATGLTH IIETRKVLDL RINLKPSYLV VPQTGFHHEK SDLLILDFGT
FQLNSKDQGL QKTTNSSLEE IMDKAYDKFD VEIKNVQLLF ARAEETWKKC RFQHPSTMHI
LQPMDIHVEL AKAMVEKDIR MARFKVSGGL PLMHVRISDQ KMKDVLYLMN SIPLPQKSSA
QSPERQVSSI PIISGGTKGL LGTSLLLDTV ESESDDEYFD AEDGEPQTCK SMKGSELKKA
AEVPNEELIN LLLKFEIKEV ILEFTKQQKE EDTILVFNVT QLGTEATMRT FDLTVVSYLK
KISLDYHEIE GSKRKPLHLI SSSDKPGLDL LKVEYIKADK NGPSFQTAFG KTEQTVKVAF
SSLNLLLQTQ ALVASINYLT TIIPSDDQSI SVAKEVQIST EKQQKNSTLP KAIVSSRDSD
IIDFRLFAKL NAFCVIVCNE KNNIAEIKIQ GLDSSLSLQS RKQSLFARLE NIIVTDVDPK
TVHKKAVSIM GNEVFRFNLD LYPDATEGDL YTDMSKVDGV LSLNVGCIQI VYLHKFLMSL
LNFLNNFQTA KESLSAATAQ AAERAATSVK DLAQRSFRVS INIDLKAPVI VIPQSSISTN
AVVVDLGLIR VHNQFSLVSD EDYLNPPVID RMDVQLTKLT LYRTVIQPGI YHPDIQLLHP
INLEFLVNRN LAASWYHKVP VVEIKGHLDS MNVSLNQEDL NLLFRILTEN LCEGTEDLDK
VKPRVQETGE IKEPLEISIS QDVHDSKNTL TTGVEEIRSV DIINMLLNFE IKEVVVTLMK
KSEKKGRPLH ELNVLQLGME AKVKTYDMTA KAYLKKISMQ CFDFTDSKGE PLHIINSSNV
TDEPLLKMLL TKADSDGPEF KTIHDSTKQR LKVSFASLDL VLHLEALLSF MDFLSSAAPF
SEPSSSEKES ELKPLVGESR SIAVKAVSSN ISQKDVFDLK ITAELNAFNV FVCDQKCNIA
DIKIHGMDAS ISVKPKQTDV FARLKDIIVM NVDLQSIHKK AVSILGDEVF RFQLTLYPDA
TEGEAYADMS KVDGKLSFKV GCIQIVYVHK FFMSLLNFLN NFQTAKEALS TATVQAAERA
ASSMKDLAQK SFRLLMDINL KAPVIIIPQS SVSPNAVIAD LGLIRVENKF SLVPMEHYSL
PPVIDKMNIE LTQLKLSRTI LQASLPQNDI EILKPVNMLL SIQRNLAAAW YVQIPGMEIK
GKLKPMQVAL SEDDLTVLMK ILLENLGEAS SQPSPTQSVQ ETVRVRKVDV SSVPDHLKEQ
EDWTDSKLSM NQIVSLQFDF HFESLSIILY NNDINQESGV AFHNDSFQLG ELRLHLMASS
GKMFKDGSMN VSVKLKTCTL DDLREGIERA TSRMIDRKND QDNNSSMIDI SYKQDKNGSQ
IDAVLDKLYV CASVEFLMTV ADFFIKAVPQ SPENVAKETQ ILPRQTATGK VKIEKDDSVR
PNMTLKAMIT DPEVVFVASL TKADAPALTA SFQCNLSLST SKLEQMMEAS VRDLKVLACP
FLREKRGKNI TTVLQPCSLF MEKCTWASGK QNINIMVKEF IIKISPIILN TVLTIMAALS
PKTKEDGSKD TSKEMENLWG IKSINDYNTW FLGVDTATEI TESFKGIEHS LIEENCGVVV
ESIQVTLECG LGHRTVPLLL AESKFSGNIK NWTSLMAAVA DVTLQVHYYN EIHAVWEPLI
ERVEGKRQWN LRLDVKKNPV QDKSLLPGDD FIPEPQMAIH ISSGNTMNIT ISKSCLNVFN
NLAKGFSEGT ASTFDYSLKD RAPFTVKNAV GVPIKVKPNC NLRVMGFPEK SDIFDVDAGQ
NLELEYASMV PSSQGNLSIL SRQESSFFTL TIVPHGYTEV ANIPVARPGR RLYNVRNPNA
SHSDSVLVQI DATEGNKVIT LRSPLQIKNH FSIAFIIYKF VKNVKLLERI GIARPEEEFH
VPLDSYRCQL FIQPAGILEH QYKESTTYIS WKEELHRSRE VRCMLQCPSV EVSFLPLIVN
TVALPDELSY ICTHGEDWDV AYIIHLYPSL TLRNLLPYSL RYLLEGTAET HELAEGSTAD
VLHSRISGEI MELVLVKYQG KNWNGHFRIR DTLPEFFPVC FSSDSTEVTT VDLSVHVRRI
GSRMVLSVFS PYWLINKTTR VLQYRSEDIH VKHPADFRDI ILFSFKKKNI FTKNKVQLKI
STSAWSSSFS LDTVGSYGCV KCPANNMEYL VGVSIKMSSF NLSRIVTLTP FCTIANKSSL
ELEVGEIASD GSMPTNKWNY IASSECLPFW PESLSGKLCV RVVGCEGSSK PFFYNRQDNG
TLLSLEDLNG GILVDVNTAE HSTVITFSDY HEGSAPALIM NHTPWDILTY KQSGSPEEMV
LLPRQARLFA WADPTGTRKL TWTYAANVGE HDLLKDGCGQ FPYDANIQIH WVSFLDGRQR
VLLFTDDVAL VSKALQAEEM EQADYEITLS LHSLGLSLVN NESKQEVSYI GITSSGVVWE
VKPKQKWKPF SQKQIILLEQ SYQKHQISRD HGWIKLDNNF EVNFDKDPME MRLPIRSPIK
RDFLSGIQIE FKQSSHQRSL RARLYWLQVD NQLPGAMFPV VFHPVAPPKS IALDSEPKPF
IDVSVITRFN EYSKVLQFKY FMVLIQEMAL KIDQGFLGAI IALFTPTTDP EAERRRTKLI
QQDIDALNAE LMETSMTDMS ILSFFEHFHI SPVKLHLSLS LGSGGEESDK EKQEMFAVHS
VNLLLKSIGA TLTDVDDLIF KLAYYEIRYQ FYKRDQLIWS VVRHYSEQFL KQMYVLVLGL
DVLGNPFGLI RGLSEGVEAL FYEPFQGAVQ GPEEFAEGLV IGVRSLFGHT VGGAAGVVSR
ITGSVGKGLA AITMDKEYQQ KRREELSRQP RDFGDSLARG GKGFLRGVVG GVTGIITKPV
EGAKKEGAAG FFKGIGKGLV GAVARPTGGI VDMASSTFQG IQRAAESTEE VSSLRPPRLI
HEDGIIRPYD RQESEGSDLL ENHIKKLEGE TYRYHCAIPG SKKTILMVTN RRVLCIKEVE
ILGLMCVDWQ CPFEDFVFPP SVSENVLKIS VKEQGLFHKK DSANQGCVRK VYLKDTATAE
RACNAIEDAQ STRQQQKLMK QSSVRLLRPQ LPS
