VP13A_HUMAN
ID VP13A_HUMAN Reviewed; 3174 AA.
AC Q96RL7; Q5JSX9; Q5JSY0; Q5VYR5; Q702P4; Q709D0; Q86YF8; Q96S61; Q9H995;
AC Q9Y2J1;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Intermembrane lipid transfer protein VPS13A {ECO:0000303|PubMed:30093493};
DE AltName: Full=Chorea-acanthocytosis protein {ECO:0000303|PubMed:11381253};
DE AltName: Full=Chorein {ECO:0000303|PubMed:11381254};
DE AltName: Full=Vacuolar protein sorting-associated protein 13A {ECO:0000305};
GN Name=VPS13A; Synonyms=CHAC, KIAA0986;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND VARIANTS CHAC LYS-90;
RP PRO-1452 AND CYS-2721.
RX PubMed=11381253; DOI=10.1038/88821;
RA Rampoldi L., Dobson-Stone C., Rubio J., Danek A., Chalmers R., Wood N.W.,
RA Verellen C., Ferrer X., Malandrini A., Fabrizi G.M., Brown R., Vance J.,
RA Pericak-Vance M., Rudolf G., Carre S., Alonso E., Manfredi M., Nemeth A.H.,
RA Monaco A.P.;
RT "A conserved sorting-associated protein is mutant in chorea-
RT acanthocytosis.";
RL Nat. Genet. 28:119-120(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=11381254; DOI=10.1038/88825;
RA Ueno S., Maruki Y., Nakamura M., Tomemori Y., Kamae K., Tanabe H.,
RA Yamashita Y., Matsuda S., Kaneko S., Sano A.;
RT "The gene encoding a newly discovered protein, chorein, is mutated in
RT chorea-acanthocytosis.";
RL Nat. Genet. 28:121-122(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), AND TISSUE SPECIFICITY.
RC TISSUE=Lymphoblast;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1638-3174 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1749-2127, AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1850-3174 (ISOFORM 2).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2200-3174.
RC TISSUE=Teratocarcinoma;
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 [8]
RP IDENTIFICATION BY 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 SER-1416, AND IDENTIFICATION BY
RP 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 [10]
RP IDENTIFICATION BY 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 [11]
RP SUBCELLULAR LOCATION, DOMAIN FFAT MOTIF, AND MUTAGENESIS OF
RP 843-PHE-PHE-844.
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).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAB7A.
RX PubMed=30709847; DOI=10.1242/dmm.036681;
RA Munoz-Braceras S., Tornero-Ecija A.R., Vincent O., Escalante R.;
RT "VPS13A is closely associated with mitochondria and is required for
RT efficient lysosomal degradation.";
RL Dis. Model. Mech. 12:0-0(2019).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VAPA AND VAPB, DOMAIN FFAT
RP MOTIF, AND MUTAGENESIS OF GLU-842.
RX PubMed=30741634; DOI=10.7554/elife.43561;
RA Yeshaw W.M., van der Zwaag M., Pinto F., Lahaye L.L., Faber A.I.,
RA Gomez-Sanchez R., Dolga A.M., Poland C., Monaco A.P., van Ijzendoorn S.C.,
RA Grzeschik N.A., Velayos-Baeza A., Sibon O.C.;
RT "Human VPS13A is associated with multiple organelles and influences
RT mitochondrial morphology and lipid droplet motility.";
RL Elife 8:0-0(2019).
RN [14]
RP INTERACTION WITH XK, AND TISSUE SPECIFICITY.
RX PubMed=31086825; DOI=10.1212/nxg.0000000000000328;
RA Urata Y., Nakamura M., Sasaki N., Shiokawa N., Nishida Y., Arai K.,
RA Hiwatashi H., Yokoyama I., Narumi S., Terayama Y., Murakami T., Ugawa Y.,
RA Sakamoto H., Kaneko S., Nakazawa Y., Yamasaki R., Sadashima S., Sakai T.,
RA Arai H., Sano A.;
RT "Novel pathogenic XK mutations in McLeod syndrome and interaction between
RT XK protein and chorein.";
RL Neurol. Genet. 5:e328-e328(2019).
RN [15]
RP FUNCTION, AND DOMAIN C-TERMINAL PART.
RX PubMed=34830155; DOI=10.3390/ijms222212274;
RA Kolakowski D., Rzepnikowska W., Kaniak-Golik A., Zoladek T., Kaminska J.;
RT "The GTPase Arf1 Is a Determinant of Yeast Vps13 Localization to the Golgi
RT Apparatus.";
RL Int. J. Mol. Sci. 22:12274-12274(2021).
RN [16]
RP VARIANTS CHAC PRO-1095 AND ARG-2460, AND VARIANTS LEU-565; ALA-898;
RP LYS-1490; CYS-1587; ILE-1973; THR-2486 AND LEU-3172.
RX PubMed=12404112; DOI=10.1038/sj.ejhg.5200866;
RA Dobson-Stone C., Danek A., Rampoldi L., Hardie R.J., Chalmers R.M.,
RA Wood N.W., Bohlega S., Dotti M.T., Federico A., Shizuka M., Tanaka M.,
RA Watanabe M., Ikeda Y., Brin M., Goldfarb L.G., Karp B.I., Mohiddin S.,
RA Fananapazir L., Storch A., Fryer A.E., Maddison P., Sibon I.,
RA Trevisol-Bittencourt P.C., Singer C., Caballero I.R., Aasly J.O.,
RA Schmierer K., Dengler R., Hiersemenzel L.-P., Zeviani M., Meiner V.,
RA Lossos A., Johnson S., Mercado F.C., Sorrentino G., Dupre N., Rouleau G.A.,
RA Volkmann J., Arpa J., Lees A., Geraud G., Chouinard S., Nemeth A.,
RA Monaco A.P.;
RT "Mutational spectrum of the CHAC gene in patients with chorea-
RT acanthocytosis.";
RL Eur. J. Hum. Genet. 10:773-781(2002).
RN [17]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-161.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [18]
RP VARIANTS CHAC PRO-67; 208-ARG--LEU-3174 DEL; 310-GLN--LEU-3174 DEL;
RP 435-TRP--LEU-3174 DEL; 712-GLN--LEU-3174 DEL; 731-ARG--LEU-3174 DEL;
RP 1297-ARG--LEU-3174 DEL; 1332-PHE--LEU-3174 DEL; 1471-ARG--LEU-3174 DEL;
RP 1921-ARG--LEU-3174 DEL; 2033-SER--LEU-3174 DEL; 2471-GLN--LEU-3174 DEL;
RP 2623-ARG--LEU-3174 DEL; 3037-ARG--LEU-3174 DEL AND 3135-ARG--LEU-3174 DEL.
RX PubMed=21598378; DOI=10.1002/ajmg.b.31206;
RA Tomiyasu A., Nakamura M., Ichiba M., Ueno S., Saiki S., Morimoto M.,
RA Kobal J., Kageyama Y., Inui T., Wakabayashi K., Yamada T., Kanemori Y.,
RA Jung H.H., Tanaka H., Orimo S., Afawi Z., Blatt I., Aasly J., Ujike H.,
RA Babovic-Vuksanovic D., Josephs K.A., Tohge R., Rodrigues G.R., Dupre N.,
RA Yamada H., Yokochi F., Kotschet K., Takei T., Rudzinska M., Szczudlik A.,
RA Penco S., Fujiwara M., Tojo K., Sano A.;
RT "Novel pathogenic mutations and copy number variations in the VPS13A gene
RT in patients with chorea-acanthocytosis.";
RL Am. J. Med. Genet. B Neuropsychiatr. Genet. 156B:620-631(2011).
RN [19]
RP VARIANTS CHAC 267-ARG--LEU-3174 DEL; 845-ASP--LEU-3174 DEL;
RP 865-ARG--LEU-3174 DEL; 1188-GLN--LEU-3174 DEL; 1471-ARG--LEU-3174 DEL AND
RP 1961-ARG--LEU-3174 DEL.
RX PubMed=31192303; DOI=10.1212/nxg.0000000000000332;
RA Nishida Y., Nakamura M., Urata Y., Kasamo K., Hiwatashi H., Yokoyama I.,
RA Mizobuchi M., Sakurai K., Osaki Y., Morita Y., Watanabe M., Yoshida K.,
RA Yamane K., Miyakoshi N., Okiyama R., Ueda T., Wakasugi N., Saitoh Y.,
RA Sakamoto T., Takahashi Y., Shibano K., Tokuoka H., Hara A., Monma K.,
RA Ogata K., Kakuda K., Mochizuki H., Arai T., Araki M., Fujii T., Tsukita K.,
RA Sakamaki-Tsukita H., Sano A.;
RT "Novel pathogenic VPS13A gene mutations in Japanese patients with chorea-
RT acanthocytosis.";
RL Neurol. Genet. 5:e332-e332(2019).
RN [20]
RP CHARACTERIZATION OF VARIANTS CHAC LYS-90 AND ARG-2460, INTERACTION WITH XK,
RP AND SUBCELLULAR LOCATION.
RX PubMed=32845802; DOI=10.1091/mbc.e19-08-0439-t;
RA Park J.S., Neiman A.M.;
RT "XK is a partner for VPS13A: a molecular link between Chorea-Acanthocytosis
RT and McLeod Syndrome.";
RL Mol. Biol. Cell 31:2425-2436(2020).
CC -!- FUNCTION: Mediates the transfer of lipids between membranes at
CC organelle contact sites (By similarity). Binds phospholipids
CC (PubMed:34830155). Required for the formation or stabilization of ER-
CC mitochondria contact sites which enable transfer of lipids between the
CC ER and mitochondria (PubMed:30741634). Negatively regulates lipid
CC droplet size and motility (PubMed:30741634). Required for efficient
CC lysosomal protein degradation (PubMed:30709847).
CC {ECO:0000250|UniProtKB:Q07878, ECO:0000269|PubMed:30709847,
CC ECO:0000269|PubMed:30741634, ECO:0000269|PubMed:34830155}.
CC -!- SUBUNIT: Interacts (via FFAT motif) with VAPA and VAPB
CC (PubMed:30741634). Interacts with RAB7A (PubMed:30709847). Interacts
CC with XK (PubMed:31086825, PubMed:32845802).
CC {ECO:0000269|PubMed:30709847, ECO:0000269|PubMed:30741634,
CC ECO:0000269|PubMed:31086825, ECO:0000269|PubMed:32845802,
CC ECO:0000269|PubMed:34830155}.
CC -!- INTERACTION:
CC Q96RL7; P16333: NCK1; NbExp=3; IntAct=EBI-1752583, EBI-389883;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:30093493, ECO:0000269|PubMed:30709847,
CC ECO:0000269|PubMed:30741634}; Peripheral membrane protein
CC {ECO:0000269|PubMed:30741634}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:30709847, ECO:0000269|PubMed:30741634,
CC ECO:0000269|PubMed:32845802}; Peripheral membrane protein
CC {ECO:0000269|PubMed:30741634}. Endosome membrane
CC {ECO:0000269|PubMed:30709847}; Peripheral membrane protein
CC {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:30709847};
CC Peripheral membrane protein {ECO:0000305}. Lipid droplet
CC {ECO:0000269|PubMed:30093493, ECO:0000269|PubMed:30709847,
CC ECO:0000269|PubMed:30741634, ECO:0000269|PubMed:32845802}. Golgi
CC apparatus {ECO:0000250|UniProtKB:Q5H8C4}. Cytoplasmic vesicle,
CC secretory vesicle, neuronal dense core vesicle
CC {ECO:0000250|UniProtKB:Q5H8C4}. Note=Localizes at mitochondria-
CC endosomes and mitochondria-endoplasmic reticulum contact sites
CC (PubMed:30741634, PubMed:30709847, PubMed:30093493).
CC {ECO:0000269|PubMed:30093493, ECO:0000269|PubMed:30709847,
CC ECO:0000269|PubMed:30741634}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=A;
CC IsoId=Q96RL7-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q96RL7-2; Sequence=VSP_006550;
CC Name=3; Synonyms=Chorein 2A;
CC IsoId=Q96RL7-3; Sequence=VSP_014904;
CC Name=4; Synonyms=Chorein 1D;
CC IsoId=Q96RL7-4; Sequence=VSP_014905, VSP_014906;
CC -!- TISSUE SPECIFICITY: Expressed in red blood cells (at protein level)
CC (PubMed:31086825). Widely expressed, with high expression in brain,
CC heart, skeletal muscle and kidney (PubMed:15498460).
CC {ECO:0000269|PubMed:15498460, ECO:0000269|PubMed:31086825}.
CC -!- DOMAIN: The C-terminal part (3058-3174) is involved in phospholipid
CC binding, including phosphatidylinositol 4,5-bisphosphate.
CC {ECO:0000269|PubMed:34830155}.
CC -!- DOMAIN: The FFAT motif is required for interaction with VAPA and VAPB
CC and its localization to the endoplasmic reticulum.
CC {ECO:0000269|PubMed:30093493, ECO:0000269|PubMed:30741634}.
CC -!- DISEASE: Choreoacanthocytosis (CHAC) [MIM:200150]: An autosomal
CC recessive neurodegenerative disorder characterized by the gradual onset
CC of hyperkinetic movements and abnormal erythrocyte morphology. Basal
CC ganglia atrophy in the brain is a pathological feature of the disease.
CC Other clinical symptoms include psychiatric features, epilepsy,
CC peripheral neuropathy, myopathy and oral self-mutilation.
CC {ECO:0000269|PubMed:11381253, ECO:0000269|PubMed:12404112,
CC ECO:0000269|PubMed:21598378, ECO:0000269|PubMed:31192303,
CC ECO:0000269|PubMed:32845802}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the VPS13 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH20576.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF337532; AAK61861.1; -; mRNA.
DR EMBL; AB054005; BAB59128.1; -; mRNA.
DR EMBL; AJ608769; CAE75581.1; -; mRNA.
DR EMBL; AJ626859; CAF25186.1; -; mRNA.
DR EMBL; AL158159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB023203; BAA76830.1; -; mRNA.
DR EMBL; BC020576; AAH20576.1; ALT_SEQ; mRNA.
DR EMBL; BC041852; AAH41852.1; -; mRNA.
DR EMBL; AK022967; BAB14337.1; -; mRNA.
DR CCDS; CCDS47983.1; -. [Q96RL7-4]
DR CCDS; CCDS55321.1; -. [Q96RL7-3]
DR CCDS; CCDS6655.1; -. [Q96RL7-1]
DR CCDS; CCDS6656.1; -. [Q96RL7-2]
DR RefSeq; NP_001018047.1; NM_001018037.1. [Q96RL7-3]
DR RefSeq; NP_001018048.1; NM_001018038.2. [Q96RL7-4]
DR RefSeq; NP_056001.1; NM_015186.3. [Q96RL7-2]
DR RefSeq; NP_150648.2; NM_033305.2. [Q96RL7-1]
DR BioGRID; 116835; 100.
DR IntAct; Q96RL7; 24.
DR MINT; Q96RL7; -.
DR STRING; 9606.ENSP00000353422; -.
DR TCDB; 9.B.416.1.1; the chorcin or vps13a (chorcin) family.
DR CarbonylDB; Q96RL7; -.
DR GlyConnect; 1889; 11 N-Linked glycans (1 site).
DR GlyGen; Q96RL7; 1 site, 11 N-linked glycans (1 site).
DR iPTMnet; Q96RL7; -.
DR PhosphoSitePlus; Q96RL7; -.
DR BioMuta; VPS13A; -.
DR DMDM; 71152975; -.
DR EPD; Q96RL7; -.
DR jPOST; Q96RL7; -.
DR MassIVE; Q96RL7; -.
DR MaxQB; Q96RL7; -.
DR PaxDb; Q96RL7; -.
DR PeptideAtlas; Q96RL7; -.
DR PRIDE; Q96RL7; -.
DR ProteomicsDB; 77984; -. [Q96RL7-1]
DR ProteomicsDB; 77985; -. [Q96RL7-2]
DR ProteomicsDB; 77986; -. [Q96RL7-3]
DR ProteomicsDB; 77987; -. [Q96RL7-4]
DR Antibodypedia; 12840; 35 antibodies from 13 providers.
DR DNASU; 23230; -.
DR Ensembl; ENST00000360280.8; ENSP00000353422.3; ENSG00000197969.14. [Q96RL7-1]
DR Ensembl; ENST00000376636.7; ENSP00000365823.3; ENSG00000197969.14. [Q96RL7-3]
DR Ensembl; ENST00000643348.1; ENSP00000493592.1; ENSG00000197969.14. [Q96RL7-2]
DR Ensembl; ENST00000645632.1; ENSP00000496361.1; ENSG00000197969.14. [Q96RL7-4]
DR GeneID; 23230; -.
DR KEGG; hsa:23230; -.
DR MANE-Select; ENST00000360280.8; ENSP00000353422.3; NM_033305.3; NP_150648.2.
DR UCSC; uc004akp.5; human. [Q96RL7-1]
DR CTD; 23230; -.
DR DisGeNET; 23230; -.
DR GeneCards; VPS13A; -.
DR GeneReviews; VPS13A; -.
DR HGNC; HGNC:1908; VPS13A.
DR HPA; ENSG00000197969; Low tissue specificity.
DR MalaCards; VPS13A; -.
DR MIM; 200150; phenotype.
DR MIM; 605978; gene.
DR neXtProt; NX_Q96RL7; -.
DR OpenTargets; ENSG00000197969; -.
DR Orphanet; 2388; Choreoacanthocytosis.
DR PharmGKB; PA26444; -.
DR VEuPathDB; HostDB:ENSG00000197969; -.
DR eggNOG; KOG1809; Eukaryota.
DR GeneTree; ENSGT00950000183083; -.
DR HOGENOM; CLU_000135_1_1_1; -.
DR InParanoid; Q96RL7; -.
DR OMA; IFFVDPS; -.
DR OrthoDB; 4159at2759; -.
DR PhylomeDB; Q96RL7; -.
DR TreeFam; TF300316; -.
DR PathwayCommons; Q96RL7; -.
DR SignaLink; Q96RL7; -.
DR BioGRID-ORCS; 23230; 25 hits in 1083 CRISPR screens.
DR ChiTaRS; VPS13A; human.
DR GeneWiki; VPS13A; -.
DR GenomeRNAi; 23230; -.
DR Pharos; Q96RL7; Tbio.
DR PRO; PR:Q96RL7; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q96RL7; protein.
DR Bgee; ENSG00000197969; Expressed in jejunal mucosa and 196 other tissues.
DR ExpressionAtlas; Q96RL7; baseline and differential.
DR Genevisible; Q96RL7; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0099013; C:neuronal dense core vesicle lumen; ISS:UniProtKB.
DR GO; GO:0097225; C:sperm midpiece; IEA:Ensembl.
DR GO; GO:0006914; P:autophagy; IMP:dictyBase.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0006895; P:Golgi to endosome transport; NAS:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:1905146; P:lysosomal protein catabolic process; IMP:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; NAS: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 GO; GO:0035176; P:social behavior; IEA:Ensembl.
DR GO; GO:0030382; P:sperm mitochondrion organization; 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; 1.
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; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Disease variant;
KW Endoplasmic reticulum; Endosome; Epilepsy; Golgi apparatus; Lipid droplet;
KW Lipid transport; Lysosome; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Neurodegeneration; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Transport.
FT CHAIN 1..3174
FT /note="Intermembrane lipid transfer protein VPS13A"
FT /id="PRO_0000106277"
FT DOMAIN 3..116
FT /note="Chorein N-terminal"
FT /evidence="ECO:0000255"
FT REPEAT 212..245
FT /note="TPR 1"
FT REPEAT 373..406
FT /note="TPR 2"
FT REPEAT 537..575
FT /note="TPR 3"
FT REPEAT 1256..1289
FT /note="TPR 4"
FT REPEAT 1291..1320
FT /note="TPR 5"
FT REPEAT 2009..2041
FT /note="TPR 6"
FT DOMAIN 2209..2454
FT /note="SHR-BD"
FT /evidence="ECO:0000255"
FT REPEAT 2568..2601
FT /note="TPR 7"
FT REPEAT 2717..2751
FT /note="TPR 8"
FT REPEAT 2860..2898
FT /note="TPR 9"
FT REPEAT 3086..3119
FT /note="TPR 10"
FT REGION 2751..3174
FT /note="Required for mitochondrial localization"
FT /evidence="ECO:0000269|PubMed:30093493,
FT ECO:0000269|PubMed:30741634"
FT REGION 2953..3027
FT /note="Required for lipid droplet localization"
FT /evidence="ECO:0000269|PubMed:30093493"
FT MOTIF 842..848
FT /note="FFAT"
FT /evidence="ECO:0000269|PubMed:30741634"
FT MOD_RES 839
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5H8C4"
FT MOD_RES 1416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1040..1078
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15498460"
FT /id="VSP_014904"
FT VAR_SEQ 3064..3174
FT /note="VMENGRFAKYKYFTHVMINKTDMLMITRRGVLFVTKGTFGQLTCEWQYSFDE
FT FTKEPFIVHGRRLRIEAKERVKSVFHAREFGKIINFKTPEDARWILTKLQEAREPSPSL
FT -> KIQFYREWIMTHSSSSDDDDDDDDDDESDLNH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10231032,
FT ECO:0000303|PubMed:11381254, ECO:0000303|PubMed:15489334"
FT /id="VSP_006550"
FT VAR_SEQ 3064..3069
FT /note="VMENGR -> ASKSLI (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15498460"
FT /id="VSP_014905"
FT VAR_SEQ 3070..3174
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15498460"
FT /id="VSP_014906"
FT VARIANT 67
FT /note="L -> P (in CHAC)"
FT /evidence="ECO:0000269|PubMed:21598378"
FT /id="VAR_086164"
FT VARIANT 90
FT /note="I -> K (in CHAC; disrupts subcellular localization
FT with protein XK on lipid droplets.; dbSNP:rs119477052)"
FT /evidence="ECO:0000269|PubMed:11381253,
FT ECO:0000269|PubMed:32845802"
FT /id="VAR_038420"
FT VARIANT 161
FT /note="R -> H (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036324"
FT VARIANT 208..3174
FT /note="Missing (in CHAC; dbSNP:rs119477053)"
FT /evidence="ECO:0000269|PubMed:21598378"
FT /id="VAR_086165"
FT VARIANT 267..3174
FT /note="Missing (in CHAC; dbSNP:rs771004767)"
FT /evidence="ECO:0000269|PubMed:31192303"
FT /id="VAR_086166"
FT VARIANT 310..3174
FT /note="Missing (in CHAC)"
FT /evidence="ECO:0000269|PubMed:21598378"
FT /id="VAR_086167"
FT VARIANT 435..3174
FT /note="Missing (in CHAC; dbSNP:rs761923202)"
FT /evidence="ECO:0000269|PubMed:21598378"
FT /id="VAR_086168"
FT VARIANT 565
FT /note="F -> L"
FT /evidence="ECO:0000269|PubMed:12404112"
FT /id="VAR_058114"
FT VARIANT 712..3174
FT /note="Missing (in CHAC)"
FT /evidence="ECO:0000269|PubMed:21598378"
FT /id="VAR_086169"
FT VARIANT 731..3174
FT /note="Missing (in CHAC; dbSNP:rs771943305)"
FT /evidence="ECO:0000269|PubMed:21598378"
FT /id="VAR_086170"
FT VARIANT 845..3174
FT /note="Missing (in CHAC)"
FT /evidence="ECO:0000269|PubMed:31192303"
FT /id="VAR_086171"
FT VARIANT 865..3174
FT /note="Missing (in CHAC; dbSNP:rs766404788)"
FT /evidence="ECO:0000269|PubMed:31192303"
FT /id="VAR_086172"
FT VARIANT 898
FT /note="V -> A (in dbSNP:rs78048112)"
FT /evidence="ECO:0000269|PubMed:12404112"
FT /id="VAR_058115"
FT VARIANT 1095
FT /note="A -> P (in CHAC)"
FT /evidence="ECO:0000269|PubMed:12404112"
FT /id="VAR_058116"
FT VARIANT 1188..3174
FT /note="Missing (in CHAC)"
FT /evidence="ECO:0000269|PubMed:31192303"
FT /id="VAR_086173"
FT VARIANT 1297..3174
FT /note="Missing (in CHAC; dbSNP:rs200280742)"
FT /evidence="ECO:0000269|PubMed:21598378"
FT /id="VAR_086174"
FT VARIANT 1332..3174
FT /note="Missing (in CHAC)"
FT /evidence="ECO:0000269|PubMed:21598378"
FT /id="VAR_086175"
FT VARIANT 1452
FT /note="S -> P (in CHAC)"
FT /evidence="ECO:0000269|PubMed:11381253"
FT /id="VAR_012803"
FT VARIANT 1471..3174
FT /note="Missing (in CHAC; dbSNP:rs1193250444)"
FT /evidence="ECO:0000269|PubMed:21598378,
FT ECO:0000269|PubMed:31192303"
FT /id="VAR_086176"
FT VARIANT 1490
FT /note="R -> K (in dbSNP:rs76077278)"
FT /evidence="ECO:0000269|PubMed:12404112"
FT /id="VAR_058117"
FT VARIANT 1587
FT /note="Y -> C (in dbSNP:rs149840356)"
FT /evidence="ECO:0000269|PubMed:12404112"
FT /id="VAR_058118"
FT VARIANT 1921..3174
FT /note="Missing (in CHAC; dbSNP:rs1369905878)"
FT /evidence="ECO:0000269|PubMed:21598378"
FT /id="VAR_086177"
FT VARIANT 1961..3174
FT /note="Missing (in CHAC)"
FT /evidence="ECO:0000269|PubMed:31192303"
FT /id="VAR_086178"
FT VARIANT 1973
FT /note="V -> I (in dbSNP:rs41289969)"
FT /evidence="ECO:0000269|PubMed:12404112"
FT /id="VAR_058119"
FT VARIANT 2033..3174
FT /note="Missing (in CHAC)"
FT /evidence="ECO:0000269|PubMed:21598378"
FT /id="VAR_086179"
FT VARIANT 2460
FT /note="W -> R (in CHAC; abolishes association with lipid
FT droplets and disrupts subcellular localization with protein
FT XK on lipid droplets.; dbSNP:rs1400127478)"
FT /evidence="ECO:0000269|PubMed:12404112,
FT ECO:0000269|PubMed:32845802"
FT /id="VAR_058120"
FT VARIANT 2471..3174
FT /note="Missing (in CHAC)"
FT /evidence="ECO:0000269|PubMed:21598378"
FT /id="VAR_086180"
FT VARIANT 2486
FT /note="I -> T (in dbSNP:rs141138349)"
FT /evidence="ECO:0000269|PubMed:12404112"
FT /id="VAR_058121"
FT VARIANT 2623..3174
FT /note="Missing (in CHAC; dbSNP:rs1055609567)"
FT /evidence="ECO:0000269|PubMed:21598378"
FT /id="VAR_086181"
FT VARIANT 2721
FT /note="Y -> C (in CHAC; dbSNP:rs781395681)"
FT /evidence="ECO:0000269|PubMed:11381253"
FT /id="VAR_038421"
FT VARIANT 3037..3174
FT /note="Missing (in CHAC; dbSNP:rs199807227)"
FT /evidence="ECO:0000269|PubMed:21598378"
FT /id="VAR_086182"
FT VARIANT 3135..3174
FT /note="Missing (in CHAC; dbSNP:rs148173878)"
FT /evidence="ECO:0000269|PubMed:21598378"
FT /id="VAR_086183"
FT VARIANT 3172
FT /note="P -> L (in dbSNP:rs75740713)"
FT /evidence="ECO:0000269|PubMed:12404112"
FT /id="VAR_058122"
FT MUTAGEN 842
FT /note="E->A: Reduced interaction with VAPA."
FT /evidence="ECO:0000269|PubMed:30741634"
FT MUTAGEN 843..844
FT /note="FF->LI: Abnormal localization to the cytosol."
FT /evidence="ECO:0000269|PubMed:30093493"
FT CONFLICT 1198
FT /note="K -> R (in Ref. 1; AAK61861)"
FT /evidence="ECO:0000305"
FT CONFLICT 1850
FT /note="L -> R (in Ref. 6; AAH41852)"
FT /evidence="ECO:0000305"
FT CONFLICT 1880
FT /note="I -> F (in Ref. 6; AAH41852)"
FT /evidence="ECO:0000305"
FT CONFLICT 2281
FT /note="G -> E (in Ref. 7; BAB14337)"
FT /evidence="ECO:0000305"
FT CONFLICT 2354
FT /note="K -> R (in Ref. 6; AAH41852)"
FT /evidence="ECO:0000305"
FT CONFLICT 2413
FT /note="T -> R (in Ref. 7; BAB14337)"
FT /evidence="ECO:0000305"
FT CONFLICT 2567
FT /note="K -> E (in Ref. 7; BAB14337)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3174 AA; 360276 MW; 58C8EC818E3350F4 CRC64;
MVFESVVVDV LNRFLGDYVV DLDTSQLSLG IWKGAVALKN LQIKENALSQ LDVPFKVKVG
HIGNLKLIIP WKNLYTQPVE AVLEEIYLLI VPSSRIKYDP LKEEKQLMEA KQQELKRIEE
AKQKVVDQEQ HLPEKQDTFA EKLVTQIIKN LQVKISSIHI RYEDDITNRD KPLSFGISLQ
NLSMQTTDQY WVPCLHDETE KLVRKLIRLD NLFAYWNVKS QMFYLSDYDN SLDDLKNGIV
NENIVPEGYD FVFRPISANA KLVMNRRSDF DFSAPKINLE IELHNIAIEF NKPQYFSIME
LLESVDMMAQ NLPYRKFKPD VPLHHHAREW WAYAIHGVLE VNVCPRLWMW SWKHIRKHRQ
KVKQYKELYK KKLTSKKPPG ELLVSLEELE KTLDVFNITI ARQTAEVEVK KAGYKIYKEG
VKDPEDNKGW FSWLWSWSEQ NTNEQQPDVQ PETLEEMLTP EEKALLYEAI GYSETAVDPT
LLKTFEALKF FVHLKSMSIV LRENHQKPEL VDIVIEEFST LIVQRPGAQA IKFETKIDSF
HITGLPDNSE KPRLLSSLDD AMSLFQITFE INPLDETVSQ RCIIEAEPLE IIYDARTVNS
IVEFFRPPKE VHLAQLTAAT LTKLEEFRSK TATGLLYIIE TQKVLDLKIN LKASYIIVPQ
DGIFSPTSNL LLLDLGHLKV TSKSRSELPD VKQGEANLKE IMDRAYDSFD IQLTSVQLLY
SRVGDNWREA RKLSVSTQHI LVPMHFNLEL SKAMVFMDVR MPKFKIYGKL PLISLRISDK
KLQGIMELIE SIPKPEPVTE VSAPVKSFQI QTSTSLGTSQ ISQKIIPLLE LPSVSEDDSE
EEFFDAPCSP LEEPLQFPTG VKSIRTRKLQ KQDCSVNMTT FKIRFEVPKV LIEFYHLVGD
CELSVVEILV LGLGAEIEIR TYDLKANAFL KEFCLKCPEY LDENKKPVYL VTTLDNTMED
LLTLEYVKAE KNVPDLKSTY NNVLQLIKVN FSSLDIHLHT EALLNTINYL HNILPQSEEK
SAPVSTTETE DKGDVIKKLA LKLSTNEDII TLQILAELSC LQIFIQDQKC NISEIKIEGL
DSEMIMRPSE TEINAKLRNI IVLDSDITAI YKKAVYITGK EVFSFKMVSY MDATAGSAYT
DMNVVDIQVN LIVGCIEVVF VTKFLYSILA FIDNFQAAKQ ALAEATVQAA GMAATGVKEL
AQRSSRMALD INIKAPVVVI PQSPVSENVF VADFGLITMT NTFHMITESQ SSPPPVIDLI
TIKLSEMRLY RSRFINDAYQ EVLDLLLPLN LEVVVERNLC WEWYQEVPCF NVNAQLKPME
FILSQEDITT IFKTLHGNIW YEKDGSASPA VTKDQYSATS GVTTNASHHS GGATVVTAAV
VEVHSRALLV KTTLNISFKT DDLTMVLYSP GPKQASFTDV RDPSLKLAEF KLENIISTLK
MYTDGSTFSS FSLKNCILDD KRPHVKKATP RMIGLTVGFD KKDMMDIKYR KVRDGCVTDA
VFQEMYICAS VEFLQTVANV FLEAYTTGTA VETSVQTWTA KEEVPTQESV KWEINVIIKN
PEIVFVADMT KNDAPALVIT TQCEICYKGN LENSTMTAAI KDLQVRACPF LPVKRKGKIT
TVLQPCDLFY QTTQKGTDPQ VIDMSVKSLT LKVSPVIINT MITITSALYT TKETIPEETA
SSTAHLWEKK DTKTLKMWFL EESNETEKIA PTTELVPKGE MIKMNIDSIF IVLEAGIGHR
TVPMLLAKSR FSGEGKNWSS LINLHCQLEL EVHYYNEMFG VWEPLLEPLE IDQTEDFRPW
NLGIKMKKKA KMAIVESDPE EENYKVPEYK TVISFHSKDQ LNITLSKCGL VMLNNLVKAF
TEAATGSSAD FVKDLAPFMI LNSLGLTISV SPSDSFSVLN IPMAKSYVLK NGESLSMDYI
RTKDNDHFNA MTSLSSKLFF ILLTPVNHST ADKIPLTKVG RRLYTVRHRE SGVERSIVCQ
IDTVEGSKKV TIRSPVQIRN HFSVPLSVYE GDTLLGTASP ENEFNIPLGS YRSFIFLKPE
DENYQMCEGI DFEEIIKNDG ALLKKKCRSK NPSKESFLIN IVPEKDNLTS LSVYSEDGWD
LPYIMHLWPP ILLRNLLPYK IAYYIEGIEN SVFTLSEGHS AQICTAQLGK ARLHLKLLDY
LNHDWKSEYH IKPNQQDISF VSFTCVTEME KTDLDIAVHM TYNTGQTVVA FHSPYWMVNK
TGRMLQYKAD GIHRKHPPNY KKPVLFSFQP NHFFNNNKVQ LMVTDSELSN QFSIDTVGSH
GAVKCKGLKM DYQVGVTIDL SSFNITRIVT FTPFYMIKNK SKYHISVAEE GNDKWLSLDL
EQCIPFWPEY ASSKLLIQVE RSEDPPKRIY FNKQENCILL RLDNELGGII AEVNLAEHST
VITFLDYHDG AATFLLINHT KNELVQYNQS SLSEIEDSLP PGKAVFYTWA DPVGSRRLKW
RCRKSHGEVT QKDDMMMPID LGEKTIYLVS FFEGLQRIIL FTEDPRVFKV TYESEKAELA
EQEIAVALQD VGISLVNNYT KQEVAYIGIT SSDVVWETKP KKKARWKPMS VKHTEKLERE
FKEYTESSPS EDKVIQLDTN VPVRLTPTGH NMKILQPHVI ALRRNYLPAL KVEYNTSAHQ
SSFRIQIYRI QIQNQIHGAV FPFVFYPVKP PKSVTMDSAP KPFTDVSIVM RSAGHSQISR
IKYFKVLIQE MDLRLDLGFI YALTDLMTEA EVTENTEVEL FHKDIEAFKE EYKTASLVDQ
SQVSLYEYFH ISPIKLHLSV SLSSGREEAK DSKQNGGLIP VHSLNLLLKS IGATLTDVQD
VVFKLAFFEL NYQFHTTSDL QSEVIRHYSK QAIKQMYVLI LGLDVLGNPF GLIREFSEGV
EAFFYEPYQG AIQGPEEFVE GMALGLKALV GGAVGGLAGA ASKITGAMAK GVAAMTMDED
YQQKRREAMN KQPAGFREGI TRGGKGLVSG FVSGITGIVT KPIKGAQKGG AAGFFKGVGK
GLVGAVARPT GGIIDMASST FQGIKRATET SEVESLRPPR FFNEDGVIRP YRLRDGTGNQ
MLQVMENGRF AKYKYFTHVM INKTDMLMIT RRGVLFVTKG TFGQLTCEWQ YSFDEFTKEP
FIVHGRRLRI EAKERVKSVF HAREFGKIIN FKTPEDARWI LTKLQEAREP SPSL
