ID VP13D_HUMAN Reviewed; 4388 AA. AC Q5THJ4; J3KP14; Q58F10; Q6MZK9; Q6ZV12; Q709C4; Q709C5; Q86UB4; Q9NSJ3; AC Q9UIM0; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2014, sequence version 2. DT 09-APR-2025, entry version 155. DE RecName: Full=Intermembrane lipid transfer protein VPS13D {ECO:0000305}; DE AltName: Full=Vacuolar protein sorting-associated protein 13D; GN Name=VPS13D {ECO:0000312|EMBL:CAE75586.1, ECO:0000312|HGNC:HGNC:23595}; GN Synonyms=KIAA0453 {ECO:0000312|EMBL:BAA32298.3}; 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:CAE75586.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE 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] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] {ECO:0000305, ECO:0000312|EMBL:CAB82724.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-2270. RA Rhodes S., Huckle E.; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000305, ECO:0000312|EMBL:BAA32298.3} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1179-4388 (ISOFORM 1). RC TISSUE=Brain {ECO:0000312|EMBL:BAA32298.3}; RX PubMed=9455484; DOI=10.1093/dnares/4.5.345; RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., RA Nomura N., Ohara O.; RT "Characterization of cDNA clones in size-fractionated cDNA libraries from RT human brain."; RL DNA Res. 4:345-349(1997). RN [5] {ECO:0000305, ECO:0000312|EMBL:BAC86054.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2039-3635 (ISOFORM 2). RC TISSUE=Tongue {ECO:0000312|EMBL:BAC86054.1}; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2094-4388 (ISOFORM 2). RC TISSUE=Fetal kidney; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] {ECO:0000305, ECO:0000312|EMBL:AAH51804.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2980-4388. RC TISSUE=Testis {ECO:0000312|EMBL:AAH51804.1}; 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1761, 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1761 AND SER-2435, AND RP 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 [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3524, 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1042, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2435, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663; SER-1034; SER-1038; RP SER-1042; SER-1138; SER-1598; SER-1603; SER-1699; THR-1761; SER-2671; RP SER-2861; SER-2864 AND SER-2983, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663; SER-1138; SER-1341; RP THR-1761; SER-1765 AND SER-2671, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [15] RP FUNCTION, AND DOMAIN. RX PubMed=29307555; DOI=10.1016/j.cub.2017.11.064; RA Anding A.L., Wang C., Chang T.K., Sliter D.A., Powers C.M., Hofmann K., RA Youle R.J., Baehrecke E.H.; RT "Vps13D Encodes a Ubiquitin-Binding Protein that Is Required for the RT Regulation of Mitochondrial Size and Clearance."; RL Curr. Biol. 28:287-295(2018). RN [16] RP FUNCTION, INVOLVEMENT IN SCAR4, VARIANTS SCAR4 662-GLN--SER-4388 DEL; RP 1106-GLN--SER-4388 DEL; ASP-1190; LEU-1307; 1803-TYR--SER-4388 DEL; RP 2277-LEU--SER-4388 DEL; 2572-GLN--SER-4388 DEL; ILE-4107; SER-4149 AND RP VAL-4210, AND CHARACTERIZATION OF VARIANTS SCAR4 1106-GLN--SER-4388 DEL; RP ASP-1190; 1803-TYR--SER-4388 DEL AND VAL-4210. RX PubMed=29604224; DOI=10.1002/ana.25220; RA Seong E., Insolera R., Dulovic M., Kamsteeg E.J., Trinh J., Brueggemann N., RA Sandford E., Li S., Ozel A.B., Li J.Z., Jewett T., Kievit A.J.A., RA Muenchau A., Shakkottai V., Klein C., Collins C.A., Lohmann K., RA van de Warrenburg B.P., Burmeister M.; RT "Mutations in VPS13D lead to a new recessive ataxia with spasticity and RT mitochondrial defects."; RL Ann. Neurol. 83:1075-1088(2018). RN [17] RP INVOLVEMENT IN SCAR4, AND VARIANTS SCAR4 ALA-865; ASP-1200; SER-2900; RP GLN-3253; SER-3521 AND GLN-4228. RX PubMed=29518281; DOI=10.1002/ana.25204; RA Gauthier J., Meijer I.A., Lessel D., Mencacci N.E., Krainc D., Hempel M., RA Tsiakas K., Prokisch H., Rossignol E., Helm M.H., Rodan L.H., RA Karamchandani J., Carecchio M., Lubbe S.J., Telegrafi A., Henderson L.B., RA Lorenzo K., Wallace S.E., Glass I.A., Hamdan F.F., Michaud J.L., RA Rouleau G.A., Campeau P.M.; RT "Recessive mutations in VPS13D cause childhood onset movement disorders."; RL Ann. Neurol. 83:1089-1095(2018). RN [18] RP VARIANT THR-1908. RX PubMed=38160741; DOI=10.1016/j.gene.2023.148119; RA Sultan T., Scorrano G., Panciroli M., Christoforou M., Raza Alvi J., RA Di Ludovico A., Qureshi S., Efthymiou S., Salpietro V., Houlden H.; RT "Clinical and molecular heterogeneity of VPS13D-related neurodevelopmental RT and movement disorders."; RL Gene 899:148119-148119(2024). CC -!- FUNCTION: Mediates the transfer of lipids between membranes at CC organelle contact sites (By similarity). Functions in promoting CC mitochondrial clearance by mitochondrial autophagy (mitophagy), also CC possibly by positively regulating mitochondrial fission CC (PubMed:29307555, PubMed:29604224). Mitophagy plays an important role CC in regulating cell health and mitochondrial size and homeostasis. CC {ECO:0000250|UniProtKB:Q07878, ECO:0000269|PubMed:29307555, CC ECO:0000269|PubMed:29604224}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1 {ECO:0000269|PubMed:15498460}; Synonyms=1A CC {ECO:0000269|PubMed:15498460}; CC IsoId=Q5THJ4-1; Sequence=Displayed; CC Name=2 {ECO:0000269|PubMed:15498460}; Synonyms=2A CC {ECO:0000269|PubMed:15498460}; CC IsoId=Q5THJ4-2; Sequence=VSP_052249; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15498460}. CC -!- DOMAIN: The UBA domain is required for mitochondrial size regulation. CC {ECO:0000269|PubMed:29307555}. CC -!- DISEASE: Spinocerebellar ataxia, autosomal recessive 4 (SCAR4) CC [MIM:607317]: 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. SCAR4 patients manifest ataxic gait with CC spasticity and hyperreflexia of the lower limbs resulting in difficulty CC walking. The age at onset is highly variable, ranging from early CC childhood to adulthood. {ECO:0000269|PubMed:29518281, CC ECO:0000269|PubMed:29604224}. 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=BAC86054.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAE46021.1; Type=Frameshift; Evidence={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; AJ608774; CAE75586.1; -; mRNA. DR EMBL; AJ608775; CAE75587.1; -; mRNA. DR EMBL; BX784395; CAI19412.1; -; Genomic_DNA. DR EMBL; AL031276; CAI19412.1; JOINED; Genomic_DNA. DR EMBL; AL031296; CAI19412.1; JOINED; Genomic_DNA. DR EMBL; AL109757; CAI19412.1; JOINED; Genomic_DNA. DR EMBL; BX682532; CAI19412.1; JOINED; Genomic_DNA. DR EMBL; BX784396; CAI19412.1; JOINED; Genomic_DNA. DR EMBL; BX784396; CAI19414.1; -; Genomic_DNA. DR EMBL; AL031276; CAI19414.1; JOINED; Genomic_DNA. DR EMBL; AL031296; CAI19414.1; JOINED; Genomic_DNA. DR EMBL; AL109757; CAI19414.1; JOINED; Genomic_DNA. DR EMBL; BX682532; CAI19414.1; JOINED; Genomic_DNA. DR EMBL; BX784395; CAI19414.1; JOINED; Genomic_DNA. DR EMBL; AL162331; CAB82724.1; -; mRNA. DR EMBL; AB007922; BAA32298.3; -; mRNA. DR EMBL; AK125118; BAC86054.1; ALT_SEQ; mRNA. DR EMBL; BX641035; CAE46021.1; ALT_FRAME; mRNA. DR EMBL; BC028115; AAH28115.1; -; mRNA. DR EMBL; BC051804; AAH51804.1; -; mRNA. DR CCDS; CCDS30588.1; -. [Q5THJ4-1] DR CCDS; CCDS30589.1; -. [Q5THJ4-2] DR PIR; T00067; T00067. DR RefSeq; NP_056193.2; NM_015378.4. [Q5THJ4-1] DR RefSeq; NP_060626.2; NM_018156.3. [Q5THJ4-2] DR SMR; Q5THJ4; -. DR BioGRID; 120485; 71. DR IntAct; Q5THJ4; 20. DR STRING; 9606.ENSP00000478104; -. DR GlyCosmos; Q5THJ4; 1 site, 1 glycan. DR GlyGen; Q5THJ4; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q5THJ4; -. DR PhosphoSitePlus; Q5THJ4; -. DR BioMuta; VPS13D; -. DR DMDM; 74756617; -. DR jPOST; Q5THJ4; -. DR MassIVE; Q5THJ4; -. DR PaxDb; 9606-ENSP00000478104; -. DR PeptideAtlas; Q5THJ4; -. DR ProteomicsDB; 65151; -. [Q5THJ4-1] DR ProteomicsDB; 65152; -. [Q5THJ4-2] DR Pumba; Q5THJ4; -. DR Antibodypedia; 63052; 64 antibodies from 9 providers. DR DNASU; 55187; -. DR Ensembl; ENST00000613099.4; ENSP00000482233.1; ENSG00000048707.15. [Q5THJ4-2] DR Ensembl; ENST00000620676.6; ENSP00000478104.1; ENSG00000048707.15. [Q5THJ4-1] DR GeneID; 55187; -. DR KEGG; hsa:55187; -. DR MANE-Select; ENST00000620676.6; ENSP00000478104.1; NM_015378.4; NP_056193.2. DR UCSC; uc031tou.2; human. [Q5THJ4-1] DR AGR; HGNC:23595; -. DR CTD; 55187; -. DR DisGeNET; 55187; -. DR GeneCards; VPS13D; -. DR GeneReviews; VPS13D; -. DR HGNC; HGNC:23595; VPS13D. DR HPA; ENSG00000048707; Low tissue specificity. DR MalaCards; VPS13D; -. DR MIM; 607317; phenotype. DR MIM; 608877; gene. DR neXtProt; NX_Q5THJ4; -. DR OpenTargets; ENSG00000048707; -. DR Orphanet; 95434; Autosomal recessive cerebellar ataxia-movement disorder syndrome. DR PharmGKB; PA134970144; -. DR VEuPathDB; HostDB:ENSG00000048707; -. DR eggNOG; KOG1796; Eukaryota. DR eggNOG; KOG1809; Eukaryota. DR GeneTree; ENSGT00950000183083; -. DR InParanoid; Q5THJ4; -. DR OMA; IEFVMDQ; -. DR OrthoDB; 272810at2759; -. DR PhylomeDB; Q5THJ4; -. DR TreeFam; TF300316; -. DR PathwayCommons; Q5THJ4; -. DR SignaLink; Q5THJ4; -. DR BioGRID-ORCS; 55187; 590 hits in 1161 CRISPR screens. DR ChiTaRS; VPS13D; human. DR GeneWiki; VPS13D; -. DR GenomeRNAi; 55187; -. DR Pharos; Q5THJ4; Tdark. DR PRO; PR:Q5THJ4; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q5THJ4; protein. DR Bgee; ENSG00000048707; Expressed in skin of leg and 204 other cell types or tissues. DR ExpressionAtlas; Q5THJ4; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; HTP:FlyBase. DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW. DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB. DR GO; GO:1901526; P:positive regulation of mitophagy; IMP:UniProtKB. 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 CDD; cd23453; beta-trefoil_Ricin_VPS13D; 1. DR CDD; cd14306; UBA_VP13D; 1. DR FunFam; 1.10.8.10:FF:000057; Vacuolar protein sorting 13 homolog D; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR InterPro; IPR015940; UBA. DR InterPro; IPR009060; UBA-like_sf. DR InterPro; IPR041969; VP13D_UBA. DR InterPro; IPR026847; VPS13. DR InterPro; IPR026854; VPS13-like_N. DR InterPro; IPR031645; VPS13_DH-like. DR InterPro; IPR031646; VPS13_extend_chorein. DR InterPro; IPR031642; VPS13_mid_RBG. DR InterPro; IPR009543; VPS13_VAB. DR PANTHER; PTHR16166:SF141; INTERMEMBRANE LIPID TRANSFER PROTEIN VPS13D; 1. DR PANTHER; PTHR16166; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN VPS13; 1. DR Pfam; PF12624; Chorein_N; 1. DR Pfam; PF22562; UBA_7; 1. DR Pfam; PF16909; VPS13_DH-like; 1. DR Pfam; PF16908; VPS13_ext_chorein; 1. DR Pfam; PF16910; VPS13_mid_rpt; 2. DR Pfam; PF06650; VPS13_VAB; 1. DR SMART; SM00165; UBA; 1. DR SUPFAM; SSF46934; UBA-like; 1. DR PROSITE; PS50030; UBA; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Disease variant; Lipid transport; KW Neurodegeneration; Phosphoprotein; Proteomics identification; KW Reference proteome; Transport. FT CHAIN 1..4388 FT /note="Intermembrane lipid transfer protein VPS13D" FT /id="PRO_0000262951" FT DOMAIN 2..115 FT /note="Chorein N-terminal" FT /evidence="ECO:0000255" FT DOMAIN 2633..2676 FT /note="UBA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212" FT DOMAIN 3276..3558 FT /note="SHR-BD" FT /evidence="ECO:0000255" FT REGION 745..796 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1563..1582 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1741..1771 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2070..2108 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2122..2145 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 747..756 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 773..782 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2123..2144 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 663 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1034 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1038 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1042 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1138 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1341 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1598 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1603 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1699 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1761 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1765 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 2435 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692" FT MOD_RES 2671 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 2861 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2864 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2983 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 3524 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VAR_SEQ 2851..2876 FT /note="SLPLVYLRTRSTASLTNLEHQIYARA -> T (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15498460, ECO:0000303|PubMed:17974005" FT /id="VSP_052249" FT VARIANT 225 FT /note="A -> T (in dbSNP:rs12057307)" FT /id="VAR_029557" FT VARIANT 662..4388 FT /note="Missing (in SCAR4)" FT /evidence="ECO:0000269|PubMed:29604224" FT /id="VAR_081496" FT VARIANT 865 FT /note="T -> A (in SCAR4; dbSNP:rs1383958401)" FT /evidence="ECO:0000269|PubMed:29518281" FT /id="VAR_080911" FT VARIANT 1106..4388 FT /note="Missing (in SCAR4; altered mitochondrial morphology FT in patient cells)" FT /evidence="ECO:0000269|PubMed:29604224" FT /id="VAR_081497" FT VARIANT 1190 FT /note="G -> D (in SCAR4; altered mitochondrial morphology FT in patient cells; dbSNP:rs1557680919)" FT /evidence="ECO:0000269|PubMed:29604224" FT /id="VAR_081498" FT VARIANT 1200 FT /note="G -> D (in SCAR4; dbSNP:rs768331333)" FT /evidence="ECO:0000269|PubMed:29518281" FT /id="VAR_080912" FT VARIANT 1307 FT /note="M -> L (in SCAR4; uncertain significance; FT dbSNP:rs775845475)" FT /evidence="ECO:0000269|PubMed:29604224" FT /id="VAR_081499" FT VARIANT 1341 FT /note="S -> L (in dbSNP:rs12407578)" FT /id="VAR_029558" FT VARIANT 1505 FT /note="E -> V (in dbSNP:rs4845898)" FT /id="VAR_029559" FT VARIANT 1624 FT /note="I -> T (in dbSNP:rs41279454)" FT /id="VAR_062169" FT VARIANT 1707 FT /note="S -> F (in dbSNP:rs958068)" FT /id="VAR_029560" FT VARIANT 1803..4388 FT /note="Missing (in SCAR4; decreased protein abundance; FT altered mitochondrial morphology in patient cells)" FT /evidence="ECO:0000269|PubMed:29604224" FT /id="VAR_081500" FT VARIANT 1908 FT /note="I -> T (found in a patient with a neurodevelopmental FT disorder; uncertain significance; dbSNP:rs376670648)" FT /evidence="ECO:0000269|PubMed:38160741" FT /id="VAR_089207" FT VARIANT 2277..4388 FT /note="Missing (in SCAR4)" FT /evidence="ECO:0000269|PubMed:29604224" FT /id="VAR_081501" FT VARIANT 2572..4388 FT /note="Missing (in SCAR4)" FT /evidence="ECO:0000269|PubMed:29604224" FT /id="VAR_081502" FT VARIANT 2900 FT /note="L -> S (in SCAR4)" FT /evidence="ECO:0000269|PubMed:29518281" FT /id="VAR_080913" FT VARIANT 3253 FT /note="R -> Q (in SCAR4; dbSNP:rs1191625571)" FT /evidence="ECO:0000269|PubMed:29518281" FT /id="VAR_080914" FT VARIANT 3521 FT /note="N -> S (in SCAR4; dbSNP:rs1557737087)" FT /evidence="ECO:0000269|PubMed:29518281" FT /id="VAR_080915" FT VARIANT 4107 FT /note="N -> I (in SCAR4; uncertain significance)" FT /evidence="ECO:0000269|PubMed:29604224" FT /id="VAR_081503" FT VARIANT 4149 FT /note="G -> S (in SCAR4; uncertain significance; FT dbSNP:rs1645323227)" FT /evidence="ECO:0000269|PubMed:29604224" FT /id="VAR_081504" FT VARIANT 4210 FT /note="A -> V (in SCAR4; altered mitochondrial morphology FT in patient cells; dbSNP:rs746736545)" FT /evidence="ECO:0000269|PubMed:29604224" FT /id="VAR_081505" FT VARIANT 4228 FT /note="R -> Q (in SCAR4; dbSNP:rs1557478316)" FT /evidence="ECO:0000269|PubMed:29518281" FT /id="VAR_080916" FT CONFLICT 2332 FT /note="I -> V (in Ref. 6; CAE46021)" FT /evidence="ECO:0000305" FT CONFLICT 2361 FT /note="C -> R (in Ref. 6; CAE46021)" FT /evidence="ECO:0000305" FT CONFLICT 2783 FT /note="S -> G (in Ref. 1; CAE75586/CAE75587)" FT /evidence="ECO:0000305" FT CONFLICT 2876 FT /note="Missing (in Ref. 6; BAA32298)" FT /evidence="ECO:0000305" FT CONFLICT 3203 FT /note="I -> T (in Ref. 7; AAH28115)" FT /evidence="ECO:0000305" FT CONFLICT 3332 FT /note="N -> S (in Ref. 6; CAE46021)" FT /evidence="ECO:0000305" FT CONFLICT 3379 FT /note="N -> S (in Ref. 6; CAE46021)" FT /evidence="ECO:0000305" FT CONFLICT 3400 FT /note="A -> T (in Ref. 6; CAE46021)" FT /evidence="ECO:0000305" FT CONFLICT 3678 FT /note="G -> E (in Ref. 6; CAE46021)" FT /evidence="ECO:0000305" FT CONFLICT 3994 FT /note="Q -> R (in Ref. 6; CAE46021)" FT /evidence="ECO:0000305" FT CONFLICT 4268 FT /note="A -> T (in Ref. 6; CAE46021)" FT /evidence="ECO:0000305" SQ SEQUENCE 4388 AA; 491916 MW; 799681E3BE2D1DDD CRC64; MLEGLVAWVL NTYLGKYVNN LNTDQLSVAL LKGAVELENL PLKKDALKEL ELPFEVKAGF IGKVTLQIPF YRPHVDPWVI SISSLHLIGA PEKIQDFNDE KEKLLERERK KALLQALEEK WKNDRQQKGE SYWYSVTASV VTRIVENIEL KIQDVHLRFE DGVTNPSHPF AFGICIKNVS MQNAVNEPVQ KLMRKKQLDV AEFSIYWDVD CTLLGDLPQM ELQEAMARSM ESRSHHYVLE PVFASALLKR NCSKKPLRSR HSPRIDCDIQ LETIPLKLSQ LQYRQIMEFL KELERKERQV KFRRWKPKVA ISKNCREWWY FALNANLYEI REQRKRCTWD FMLHRARDAV SYTDKYFNKL KGGLLSTDDK EEMCRIEEEQ SFEELKILRE LVHDRFHKQE ELAESLREPQ FDSPGACPGA PEPGGGSGML QYLQSWFPGW GGWYGQQTPE GNVVEGLSAE QQEQWIPEEI LGTEEFFDPT ADASCMNTYT KRDHVFAKLN LQLQRGTVTL LHKEQGTPQM NESAFMQLEF SDVKLLAESL PRRNSSLLSV RLGGLFLRDL ATEGTMFPLL VFPNPQKEVG RVSQSFGLQT TSADRSDHYP AADPDGPVFE MLYERNPAHS HFERRLNVST RPLNIIYNPQ AIKKVADFFY KGKVHTSGFG YQSELELRVA EAARRQYNKL KMQTKAEIRQ TLDRLLVGDF IEESKRWTVR LDISAPQVIF PDDFKFKNPV LVVVDLGRML LTNTQDNSRR KSRDGSASEE TQFSDDEYKT PLATPPNTPP PESSSSNGEK TPPFSGVEFS EEQLQAHLMS TKMYERYSLS FMDLQIMVGR VKDNWKHVQD IDVGPTHVVE KFNVHLQLER RLIYTSDPKY PGAVLSGNLP DLKIHINEDK ISALKNCFAL LTTPEMKTSD TQIKEKIFPQ EEQRGSLQDS VMNLTQSIVL LEQHTREVLV ESQLLLAEFK VNCMQLGVES NGRYISVLKV FGTNAHFVKR PYDAEVSLTV HGLLLVDTMQ TYGADFDLLM ASHKNLSFDI PTGSLRDSRA QSPVSGPNVA HLTDGATLND RSATSVSLDK ILTKEQESLI KLEYQFVSSE CPSMNLDSTL QVISLQVNNL DIILNPETIV ELIGFLQKSF PKEKDDLSPQ PLMTDFERSF REQGTYQSTY EQNTEVAVEI HRLNLLLLRT VGMANREKYG RKIATASIGG TKVNVSMGST FDMNGSLGCL QLMDLTQDNV KNQYVVSIGN SVGYENIISD IGYFESVFVR MEDAALTEAL SFTFVERSKQ ECFLNLKMAS LHYNHSAKFL KELTLSMDEL EENFRGMLKS AATKVTTVLA TKTAEYSEMV SLFETPRKTR EPFILEENEI YGFDLASSHL DTVKLILNIN IESPVVSIPR KPGSPELLVG HLGQIFIQNF VAGDDESRSD RLQVEIKDIK LYSLNCTQLA GREAVGSEGS RMFCPPSGSG SANSQEEAHF TRHDFFESLH RGQAFHILNN TTIQFKLEKI PIERESELTF SLSPDDLGTS SIMKIEGKFV NPVQVVLAKH VYEQVLQTLD NLVYSEDLNK YPASATSSPC PDSPLPPLST CGESSVERKE NGLFSHSSLS NTSQKSLSVK EVKSFTQIQA TFCISELQVQ LSGDLTLGAQ GLVSLKFQDF EVEFSKDHPQ TLSIQIALHS LLMEDLLEKN PDSKYKNLMV SRGAPKPSSL AQKEYLSQSC PSVSNVEYPD MPRSLPSHME EAPNVFQLYQ RPTSASRKKQ KEVQDKDYPL TPPPSPTVDE PKILVGKSKF DDSLVHINIF LVDKKHPEFS SSYNRVNRSI DVDFNCLDVL ITLQTWVVIL DFFGIGSTAD NHAMRLPPEG ILHNVKLEPH ASMESGLQDP VNTKLDLKVH SLSLVLNKTT SELAKANVSK LVAHLEMIEG DLALQGSIGS LSLSDLTCHG EFYRERFTTS GEEALIFQTF KYGRPDPLLR REHDIRVSLR MASVQYVHTQ RFQAEVVAFI QHFTQLQDVL GRQRAAIEGQ TVRDQAQRCS RVLLDIEAGA PVLLIPESSR SNNLIVANLG KLKVKNKFLF AGFPGTFSLQ DKESVPSASP TGIPKHSLRK TTSTEEPRGT HSQGQFTMPL AGMSLGSLKS EFVPSTSTKQ QGPQPTLSVG QESSSPEDHV CLLDCVVVDL QDMDIFAAER HPREYSKAPE DSSGDLIFPS YFVRQTGGSL LTEPCRLKLQ VERNLDKEIS HTVPDISIHG NLSSVHCSLD LYKYKLIRGL LENNLGEPIE EFMRPYDLQD PRIHTVLSGE VYTCMCFLID MVNVSLELKD PKRKEGAGSL ARFDFKKCKL LYESFSNQTK SINLVSHSMM AFDTRYAGQK TSPGMTNVFS CIFQPAKNSS TTQGSIQIEL HFRSTKDSSC FTVVLNNLRV FLIFDWLLLV HDFLHTPSDI KKQNHVTPSR HRNSSSESAI VPKTVKSGVV TKRSSLPVSN ERHLEVKVNV TGTEFVVIED VSCFDTNAII LKGTTVLTYK PRFVDRPFSG SLFGIEVFSC RLGNEHDTAL SIVDPVQIQM ELVGNSSYQN SSGLMDAFNS EDFPPVLEIQ LQALDIRLSY NDVQLFLAIA KSIPEQANAA VPDSVALESD SVGTYLPGAS RVGEEIREGT RHTLDPVLEL QLARLQELGF SMDDCRKALL ACQGQLKKAA SWLFKNAEPL KSLSLASTSR DSPGAVAAPL ISGVEIKAES VCICFIDDCM DCDVPLAELT FSRLNFLQRV RTSPEGYAHF TLSGDYYNRA LSGWEPFIEP WPCSVSWQQQ AASRLHPPRL KLEAKAKPRL DINITSVLID QYVSTKESWM ADYCKDDKDI ESAKSEDWMG SSVDPPCFGQ SLPLVYLRTR STASLTNLEH QIYARAEVKT PKRRQPFVPF ALRNHTGCTL WFATLTTTPT RAALSHSGSP GVVPEGNGTF LDDTHNVSEW REVLTGEEIP FEFEARGKLR HRHTHDLRIH QLQVRVNGWE QVSPVSVDKV GTFFRYAAPD KNSSSSTIGS PSSRTNIIHP QVYFSSLPPV RVVFAVTMEG SARKVITVRS ALIVRNRLET PMELRLDSPS APDKPVVLPA IMPGDSFAVP LHLTSWRLQA RPKGLGVFFC KAPIHWTNVV KTAEISSSKR ECHSMDTEKS RFFRFCVAIK KENYPDYMPS NIFSDSAKQI FRQPGHTIYL LPTVVICNLL PCELDFYVKG MPINGTLKPG KEAALHTADT SQNIELGVSL ENFPLCKELL IPPGTQNYMV RMRLYDVNRR QLNLTIRIVC RAEGSLKIFI SAPYWLINKT GLPLIFRQDN AKTDAAGQFE EHELARSLSP LLFCYADKEQ PNLCTMRIGR GIHPEGMPGW CQGFSLDGGS GVRALKVIQQ GNRPGLIYNI GIDVKKGRGR YIDTCMVIFA PRYLLDNKSS HKLAFAQREF ARGQGTANPE GYISTLPGSS VVFHWPRNDY DQLLCVRLMD VPNCIWSGGF EVNKNNSFHI NMRDTLGKCF FLRVEITLRG ATYRISFSDT DQLPPPFRID NFSKVPVVFT QHGVAEPRLR TEVKPMTSLD YAWDEPTLPP FITLTVKGAG SSEINCNMND FQDNRQLYYE NFIYIAATYT FSGLQEGTGR PVASNKAITC AELVLDVSPK TQRVILKKKE PGKRSQLWRM TGTGMLAHEG SSVPHNPNKP SAARSTEGSA ILDIAGLAAV TDNRYEPLML RKPDRRRSTT QTWSFREGKL TCGLHGLVVQ AKGGLSGLFD GAEVVLGPDT SMELLGPVPP EQQFINQKMR PGSGMLSIRV IPDGPTRALQ ITDFCHRKSS RSYEVDELPV TEQELQKLKN PDTEQELEVL VRLEGGIGLS LINKVPEELV FASLTGINVH YTQLATSHML ELSIQDVQVD NQLIGTTQPF MLYVTPLSNE NEVIETGPAV QVNAVKFPSK SALTNIYKHL MITAQRFTVQ IEEKLLLKLL SFFGYDQAES EVEKYDENLH EKTAEQGGTP IRYYFENLKI SIPQIKLSVF TSNKLPLDLK ALKSTLGFPL IRFEDAVINL DPFTRVHPYE TKEFIINDIL KHFQEELLSQ AARILGSVDF LGNPMGLLND VSEGVTGLIK YGNVGGLIRN VTHGVSNSAA KFAGTLSDGL GKTMDNRHQS EREYIRYHAA TSGEHLVAGI HGLAHGIIGG LTSVITSTVE GVKTEGGVSG FISGLGKGLV GTVTKPVAGA LDFASETAQA VRDTATLSGP RTQAQRVRKP RCCTGPQGLL PRYSESQAEG QEQLFKLTDN IQDEFFIAVE NIDSYCVLIS SKAVYFLKSG DYVDREAIFL EVKYDDLYHC LVSKDHGKVY VQVTKKAVST SSGVSIPGPS HQKPMVHVKS EVLAVKLSQE INYAKSLYYE QQLMLRLSEN REQLELDS //