VP13A_MOUSE
ID VP13A_MOUSE Reviewed; 3166 AA.
AC Q5H8C4; Q3UQG7; Q3UX03; Q5DU08; Q80YV7; Q8C722;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Intermembrane lipid transfer protein VPS13A {ECO:0000250|UniProtKB:Q96RL7};
DE AltName: Full=Chorea-acanthocytosis protein homolog {ECO:0000305};
DE AltName: Full=Chorein {ECO:0000305};
DE AltName: Full=Vacuolar protein sorting-associated protein 13A {ECO:0000305};
GN Name=Vps13a {ECO:0000312|MGI:MGI:2444304};
GN Synonyms=Chac {ECO:0000312|EMBL:BAD89296.1},
GN Kiaa0986 {ECO:0000312|EMBL:BAD90423.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAD89296.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAD89296.1};
RC TISSUE=Brain {ECO:0000312|EMBL:BAD89296.1};
RX PubMed=15686477; DOI=10.1111/j.1471-4159.2004.02924.x;
RA Tomemori Y., Ichiba M., Kusumoto A., Mizuno E., Sato D., Muroya S.,
RA Nakamura M., Kawaguchi H., Yoshida H., Ueno S., Nakao K., Nakamura K.,
RA Aiba A., Katsuki M., Sano A.;
RT "A gene-targeted mouse model for chorea-acanthocytosis.";
RL J. Neurochem. 92:759-766(2005).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAE25075.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-368; 875-1696 AND 1896-2816.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE25075.1};
RC TISSUE=Egg {ECO:0000312|EMBL:BAE22761.1},
RC Kidney {ECO:0000312|EMBL:BAC35101.1}, and
RC Stomach {ECO:0000312|EMBL:BAE25075.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAD90423.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2141-3166 (ISOFORM 2).
RC TISSUE=Fetal brain {ECO:0000312|EMBL:BAD90423.1};
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH50055.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2477-3166 (ISOFORM 1).
RC TISSUE=Pancreas {ECO:0000312|EMBL:AAH50055.1};
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-831 AND SER-835, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=22366033; DOI=10.1016/j.bbrc.2012.02.047;
RA Hayashi T., Kishida M., Nishizawa Y., Iijima M., Koriyama C., Nakamura M.,
RA Sano A., Kishida S.;
RT "Subcellular localization and putative role of VPS13A/chorein in
RT dopaminergic neuronal cells.";
RL Biochem. Biophys. Res. Commun. 419:511-516(2012).
CC -!- FUNCTION: Mediates the transfer of lipids between membranes at
CC organelle contact sites (By similarity). Required for the formation or
CC stabilization of ER-mitochondria contact sites which enable transfer of
CC lipids between the ER and mitochondria (By similarity). Negatively
CC regulates lipid droplet size and motility (By similarity). Required for
CC efficient lysosomal protein degradation (By similarity).
CC {ECO:0000250|UniProtKB:Q07878, ECO:0000250|UniProtKB:Q96RL7}.
CC -!- SUBUNIT: Interacts (via FFAT motif) with VAPA and VAPB (By similarity).
CC Interacts with RAB7A (By similarity). Interacts with XK (By
CC similarity). {ECO:0000250|UniProtKB:Q96RL7}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q96RL7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96RL7}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96RL7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96RL7}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q96RL7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96RL7}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q96RL7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96RL7}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q96RL7}. Golgi apparatus
CC {ECO:0000269|PubMed:22366033}. Cytoplasmic vesicle, secretory vesicle,
CC neuronal dense core vesicle {ECO:0000269|PubMed:22366033}.
CC Note=Localizes at mitochondria-endosomes and mitochondria-endoplasmic
CC reticulum contact sites. {ECO:0000250|UniProtKB:Q96RL7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15686477};
CC IsoId=Q5H8C4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|Ref.3};
CC IsoId=Q5H8C4-2; Sequence=VSP_052241, VSP_052242;
CC -!- DOMAIN: The FFAT motif is required for interaction with VAPA and VAPB
CC and its localization to the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:Q96RL7}.
CC -!- DOMAIN: The C-terminal part (3050-3166) is involved in phospholipid
CC binding, including phosphatidylinositol 4,5-bisphosphate.
CC {ECO:0000250|UniProtKB:Q96RL7}.
CC -!- DISRUPTION PHENOTYPE: Mice show defects in motor coordination, social
CC investigation, erythrocyte morphology as well as size and morphology of
CC the striatum. Provides a mouse model for chorea-acanthocytosis (CHAC)
CC with a mild phenotype and late adult onset.
CC {ECO:0000269|PubMed:15686477}.
CC -!- SIMILARITY: Belongs to the VPS13 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE22761.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AB115421; BAD89296.1; -; mRNA.
DR EMBL; AK052697; BAC35101.1; -; mRNA.
DR EMBL; AK135983; BAE22761.1; ALT_SEQ; mRNA.
DR EMBL; AK142462; BAE25075.1; -; mRNA.
DR EMBL; AK220362; BAD90423.1; -; mRNA.
DR EMBL; BC050055; AAH50055.1; -; mRNA.
DR CCDS; CCDS37929.1; -. [Q5H8C4-1]
DR RefSeq; NP_766616.2; NM_173028.4. [Q5H8C4-1]
DR RefSeq; XP_006527189.1; XM_006527126.3. [Q5H8C4-2]
DR BioGRID; 234844; 9.
DR STRING; 10090.ENSMUSP00000068716; -.
DR iPTMnet; Q5H8C4; -.
DR PhosphoSitePlus; Q5H8C4; -.
DR EPD; Q5H8C4; -.
DR MaxQB; Q5H8C4; -.
DR PaxDb; Q5H8C4; -.
DR PeptideAtlas; Q5H8C4; -.
DR PRIDE; Q5H8C4; -.
DR ProteomicsDB; 297962; -. [Q5H8C4-1]
DR ProteomicsDB; 297963; -. [Q5H8C4-2]
DR Antibodypedia; 12840; 35 antibodies from 13 providers.
DR DNASU; 271564; -.
DR Ensembl; ENSMUST00000068156; ENSMUSP00000068716; ENSMUSG00000046230. [Q5H8C4-1]
DR GeneID; 271564; -.
DR KEGG; mmu:271564; -.
DR UCSC; uc008gwv.2; mouse. [Q5H8C4-1]
DR CTD; 23230; -.
DR MGI; MGI:2444304; Vps13a.
DR VEuPathDB; HostDB:ENSMUSG00000046230; -.
DR eggNOG; KOG1809; Eukaryota.
DR GeneTree; ENSGT00950000183083; -.
DR HOGENOM; CLU_000135_1_1_1; -.
DR InParanoid; Q5H8C4; -.
DR OMA; IFFVDPS; -.
DR PhylomeDB; Q5H8C4; -.
DR TreeFam; TF300316; -.
DR BioGRID-ORCS; 271564; 12 hits in 73 CRISPR screens.
DR ChiTaRS; Vps13a; mouse.
DR PRO; PR:Q5H8C4; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q5H8C4; protein.
DR Bgee; ENSMUSG00000046230; Expressed in spermatocyte and 212 other tissues.
DR ExpressionAtlas; Q5H8C4; baseline and differential.
DR Genevisible; Q5H8C4; MM.
DR GO; GO:0031045; C:dense core granule; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0099013; C:neuronal dense core vesicle lumen; IDA:UniProtKB.
DR GO; GO:0097225; C:sperm midpiece; IDA:MGI.
DR GO; GO:0006914; P:autophagy; ISO:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:1905146; P:lysosomal protein catabolic process; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IMP:MGI.
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; IMP:MGI.
DR GO; GO:0030382; P:sperm mitochondrion organization; IMP:MGI.
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; Endoplasmic reticulum; Endosome;
KW Golgi apparatus; Lipid droplet; Lipid transport; Lysosome; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Transport.
FT CHAIN 1..3166
FT /note="Intermembrane lipid transfer protein VPS13A"
FT /id="PRO_0000262948"
FT DOMAIN 3..116
FT /note="Chorein N-terminal"
FT /evidence="ECO:0000255"
FT REPEAT 212..245
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 373..406
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 1806..1840
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 1999..2034
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT DOMAIN 2202..2447
FT /note="SHR-BD"
FT /evidence="ECO:0000255"
FT REPEAT 2716..2750
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 2852..2890
FT /note="TPR 6"
FT /evidence="ECO:0000255"
FT REGION 1343..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2607..3166
FT /note="Required for mitochondrial localization"
FT /evidence="ECO:0000250|UniProtKB:Q96RL7"
FT REGION 2743..3166
FT /note="Required for mitochondrial localization"
FT /evidence="ECO:0000250|UniProtKB:Q96RL7"
FT REGION 2945..3019
FT /note="Required for lipid droplet localization"
FT /evidence="ECO:0000250|UniProtKB:Q96RL7"
FT MOTIF 838..844
FT /note="FFAT"
FT /evidence="ECO:0000250|UniProtKB:Q96RL7"
FT MOD_RES 831
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 835
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RL7"
FT VAR_SEQ 3056..3061
FT /note="VMENGR -> ASKSLI (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_052241"
FT VAR_SEQ 3062..3166
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_052242"
SQ SEQUENCE 3166 AA; 359401 MW; 68EFBB87EF7833B0 CRC64;
MVFESVVVEV LNRFLGDYVV NLDESQLSLG IWKGAVALKN LVIKENALHE LDVPFKVKVG
HIGSLKLKIP WKNLYTQPVE AVLEEIFLLI VPSSRIQYDP IKEEKQLMET KQQELKRIEK
AKQKVFDKEK PREEKQDTFT EKLVTQIIQN LQVQISSIHI RYEDDITNGD KPLSFGISLQ
NISLQTTDQY WIPCLHDNTE KLVRKLIRLD NLFAYWNVNS EMFYLNDYDE SLKALKNGIV
NENIVPEGYD FVFRPISASA KLQMNRRSDF DFSDPKINLA VDLHTIAIEF NKPQYFSLME
LLESIDMMTQ NQPYRKFKPS VPLHLHAKEW WAYAIHSILE VNVCPSLRMW SWEHIRNHRY
KMKRYREFYK KKLTSKKPSP EILMSLEELE KTLDVFNITI ARQQAEVEAK KAGYKIYKEG
VKDPEDNAGW FGWLWTWSES NANQQQDVKP GILEEMLTPE EKSLLYEAIG YSETAVDPTL
PKTFEALKFF VHLKSMSIVL RENHQKPELL NVVVEGLSTS VVQRPGAQAI KFETKIDSFH
ITGLPDDFKK PHLLSSLDDT SLLQITFEIN PLNETVAQRC TIEAEPLEII YDARTVNSIV
EFFRPPKDVH LAQLTSVTLT KLEEFRAKTA TGLLYVIETQ KVLDLRINVK ASYVIVPQYG
NFSPTSNLLL LDLGHLKVSS KRRSLLPDVR PSEASLEDIM HRAYDSFDIQ LTSIQLLYSR
VGDNWKEARK LNVSTQHILI PMHVNVELSK AMVFMDIKMP KFKISGKLPL VSLRISDKKL
QGIMELLGSI PKPEPVTDVS APARSFQIQA SALPVSHISQ KLIPLLEQPV TEDDSEEEFF
DAPCSPLEEC PQVSCRDKCT RQKKLQKKDC VMNLIQLRMR FEVAEVSIQF YHLVGDCELP
VLEMGALGLG TEAEFRTFDL KGSAFLKELW LKCPEYLDEN KKPVYLITTL DNTMEDLLTL
EFMKVEKNAP NLNSTYNNVL QLIKVNFSSL DIHLHTEALL NTMNYLNNIL PELREKSASV
SAAEPEDKGD IIKKLALKLP TNEDIITLQL LAELSCLQIF IQDQKQNISE IKIEGLDSEM
IMKPLVTEIN AKLRNIIVLD SDKMAIYKKA LYITGKEVFS FKMISYMDAT AGYAYTDMSV
VDIRVHLTVG CIEVVFITKF LYSILAFIDN FQAVKDALAE ATVQAAEMAA DGVKELARKS
SRFALDVNIK APVVLIPQSP VSQNVFVADF GLITMKNIFV TVTETQSNIP PVIDLITIKL
SKMRLYRSQF RNDTYQEVLD LLLPLNLEVI VERNLSWEWY KEVPCFNIKA QLKPMEFILS
QEDLTTVFQT LHGNIWYGQD LSAPSSANKD PETMTSGVTS PPDHSPATVV TAAVVEVHPQ
ASQAHTMLNV SFQTDYLTMA LYSPGPDEAS FTDVRDPSLE LAEFKLENII SSLKIYTDDS
TVFSFSVKNC ILDDKRSHVM KATPRMIGLT VGFDKKDMVD IKYRKIKTFV VTDAVVQEMY
VCASVEFLMT VAHIFFDAYM TSTALETSVQ TRTTREAPAQ ELGKWEMNIL IKNPEIVFVA
DMTRNDAPAL VITTQCEICC KGEPTSNTVT AAIKDLQVRA CPFLPVKRKG KVTTVLQPCD
LFYQATQLGR DPQMIDISVK SLTLKVSPVI INTIITITSA LYTTKETVPE ENTSNIAHLW
DKKDTKNLKM WFLEESNESE KVVPTNEVMP GGETLNLRID SIFIVLEAGI GHRTVPMLLA
KACFSGESKN WLSLINLHCH LELEVHYYNE MFGVWEPLLE PLEIDQTDDF RPWNLGIKMK
KKAKEAIVES DSEAENYKVP EYKTAISFYS RDQLNITLSK CGLVMLNNLV EAFTEAATGS
SSVFLRDLAP FMIFNSLGLT VSVSPSDSFS VLNVPLAKSY ELKNDESLSM DYVRTKDNDH
FNAMTSLSSK LFFILLTPAN HSVADKIPLT KVGRRLYTVR HRESGVERSI ICQIDTVEGS
KKVTIRSPVQ IKNHFSIPIS VFEGDTLLGI ASPENEFNIP LASYRSSLSL VPEDQDYQLC
EGIDFEEIIK YDGQLLKKKC RSTNPSKKSF VINIVPEKDN LASLSVYSED GWDLPYVLHL
WPPILIRNLL PYKVAYYIEG IENTVVTLSE GHSSQIYNVE MDQAKLHLKL LDYLNHDWKS
EFYIRSSQQD INFINFTCLT EMEKSDLDIA IHMTYNTGQT VVAFHSPYWM VNKTNRMLQY
KADGIHRKHP PNYTKPVLFS FQPNHFFNNN KVQLMVTDSE LSDQFSIDTV GSHGAIRCKG
LKMEYQVGVT INLSSFNITR IVTFIPFYMI KNKSKYHISV AEEGSDKWLS LDLEQSIPFW
PENASNILLI QVERSEDPPK RIYFNKQDNC ILLRLNNELG GIIAEVNLAE HSTVITFSDY
HDGAATFLLI NHTKSDPVQY NQSSLGEIED SLPPGKAVYY TWADPVGSRK LKWSCGQSYG
EVTHKDDMMT PISVGKKTIY LVSFFEGLQR IILFTEDPRV FKVTYESEKA ELAELEVVLA
LQDVGISLVN NYTKQEVAYI GITSSDVVWE AKPKKKARWK PMSVKHTEKL EKEFREYTEA
SPLEDKVVEL DNIPVRLTPS GNDMKILQPH VIPVRRNYLP ALKVEYNTSA HQSSFRIQIY
RIQIQNQIHG AIFPFVFYPI KPPRSVTMDS APKPFTDVSI VMRSAGHSQI SRIKYFKVLI
QEMDLSLDLG FVYALADLVT KAEVTEKTEV EHFHKDVEAF EQEYEVVSSV DQSQVNLFEY
FHISPIKLHL SVSLSSGRDE AKDSEQHGGL IPVHSLNLLL KSIGATLTDV QDVVFKLAFF
ELNYQFHTTS ELQSEVIRHY SKQAIKQMYV LILGLDVLGN PFGLIREFSE GVEAFFYEPY
QGAIQGPEEF VEGMALGLKA LVGGAVGGLA GAASKITSAM AKGVAAMTMD EDYQQKRREA
MNKQPAGLRE GITRGGKGLV SGFVSGITGI VTKPIKGAQK EGAAGFFKGV GKGLVGAVTR
PTGGIIDMAS STFQGIKRAT ETSEVESLRP PRFFNEDGVI RPYRLRDGSG NQMLQVMENG
RFAKYKYFTH VMINKTDMFM ITRRGVLFVT KGTFGQLTCE WQYTFDEFTK EPFIVHGRRL
RIEAKERVKS VFHAKEFGKI VNFKTPEDAR WILTKLEEAR EPSPRL
