VP13C_MOUSE
ID VP13C_MOUSE Reviewed; 3748 AA.
AC Q8BX70; Q3V3W5; Q6ZPE1; Q8BLB1; Q8BQI7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Intermembrane lipid transfer protein VPS13C {ECO:0000250|UniProtKB:Q709C8};
DE AltName: Full=Vacuolar protein sorting-associated protein 13C {ECO:0000305};
GN Name=Vps13c {ECO:0000312|MGI:MGI:2444207};
GN Synonyms=Kiaa3021 {ECO:0000312|EMBL:BAC98296.1};
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC32479.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-924 (ISOFORM 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1444-2010, AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 3040-3748 (ISOFORMS 1/3).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC32479.2};
RC TISSUE=Cerebellum {ECO:0000312|EMBL:BAC33451.1},
RC Corpora quadrigemina {ECO:0000312|EMBL:BAC32479.2},
RC Embryo {ECO:0000312|EMBL:BAC33809.1}, and
RC Thymus {ECO:0000312|EMBL:BAE20465.1};
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:BAC98296.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2868-3623 (ISOFORM 2).
RC TISSUE=Brain {ECO:0000312|EMBL:BAC98296.1};
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1968 AND SER-1974, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-736; SER-871;
RP SER-873 AND SER-2442, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-3514, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
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 (By similarity). Involved in the regulation of PINK1/PRKN-
CC mediated mitophagy in response to mitochondrial depolarization (By
CC similarity). {ECO:0000250|UniProtKB:Q07878,
CC ECO:0000250|UniProtKB:Q709C8}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q709C8}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q709C8}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q709C8}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q709C8}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q709C8}. Note=May localize to endoplasmic
CC reticulum-endolysosome contact sites. {ECO:0000250|UniProtKB:Q709C8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BX70-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:14621295};
CC IsoId=Q8BX70-2; Sequence=VSP_052247, VSP_052248;
CC Name=3 {ECO:0000269|PubMed:16141072};
CC IsoId=Q8BX70-3; Sequence=VSP_052246;
CC -!- DOMAIN: The FFAT motif is required for localization to the endoplasmic
CC reticulum. {ECO:0000250|UniProtKB:Q709C8}.
CC -!- SIMILARITY: Belongs to the VPS13 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC33451.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC33809.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE20465.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC156799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK030931; BAE20465.1; ALT_INIT; mRNA.
DR EMBL; AK045749; BAC32479.2; -; mRNA.
DR EMBL; AK048766; BAC33451.1; ALT_FRAME; mRNA.
DR EMBL; AK049557; BAC33809.1; ALT_INIT; mRNA.
DR EMBL; AK129486; BAC98296.1; -; mRNA.
DR CCDS; CCDS40676.1; -. [Q8BX70-1]
DR RefSeq; NP_796158.2; NM_177184.3. [Q8BX70-1]
DR RefSeq; XP_006511289.1; XM_006511226.1. [Q8BX70-2]
DR BioGRID; 236091; 5.
DR IntAct; Q8BX70; 1.
DR MINT; Q8BX70; -.
DR STRING; 10090.ENSMUSP00000077040; -.
DR iPTMnet; Q8BX70; -.
DR PhosphoSitePlus; Q8BX70; -.
DR SwissPalm; Q8BX70; -.
DR EPD; Q8BX70; -.
DR jPOST; Q8BX70; -.
DR MaxQB; Q8BX70; -.
DR PaxDb; Q8BX70; -.
DR PeptideAtlas; Q8BX70; -.
DR PRIDE; Q8BX70; -.
DR ProteomicsDB; 297964; -. [Q8BX70-1]
DR ProteomicsDB; 297965; -. [Q8BX70-2]
DR ProteomicsDB; 297966; -. [Q8BX70-3]
DR Antibodypedia; 50681; 13 antibodies from 8 providers.
DR Ensembl; ENSMUST00000077879; ENSMUSP00000077040; ENSMUSG00000035284. [Q8BX70-1]
DR GeneID; 320528; -.
DR KEGG; mmu:320528; -.
DR UCSC; uc009qms.1; mouse. [Q8BX70-1]
DR CTD; 54832; -.
DR MGI; MGI:2444207; Vps13c.
DR VEuPathDB; HostDB:ENSMUSG00000035284; -.
DR eggNOG; KOG1809; Eukaryota.
DR GeneTree; ENSGT00950000183083; -.
DR HOGENOM; CLU_000135_1_1_1; -.
DR InParanoid; Q8BX70; -.
DR OMA; VDVRDWS; -.
DR PhylomeDB; Q8BX70; -.
DR TreeFam; TF300316; -.
DR BioGRID-ORCS; 320528; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Vps13c; mouse.
DR PRO; PR:Q8BX70; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BX70; protein.
DR Bgee; ENSMUSG00000035284; Expressed in substantia nigra and 119 other tissues.
DR ExpressionAtlas; Q8BX70; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0032127; C:dense core granule membrane; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0007005; P:mitochondrion organization; ISO:MGI.
DR GO; GO:1905090; P:negative regulation of parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization; ISS: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; 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; 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; Endoplasmic reticulum; Endosome;
KW Lipid droplet; Lipid transport; Lysosome; Membrane; Methylation;
KW Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..3748
FT /note="Intermembrane lipid transfer protein VPS13C"
FT /id="PRO_0000262950"
FT DOMAIN 3..115
FT /note="Chorein N-terminal"
FT /evidence="ECO:0000255"
FT DOMAIN 2760..3012
FT /note="SHR-BD"
FT /evidence="ECO:0000255"
FT REGION 2410..3304
FT /note="Required for late endosome/lysosome localization"
FT /evidence="ECO:0000250|UniProtKB:Q709C8"
FT REGION 3305..3748
FT /note="Required for lipid droplet localization"
FT /evidence="ECO:0000250|UniProtKB:Q709C8"
FT MOTIF 876..882
FT /note="FFAT"
FT /evidence="ECO:0000305"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 613
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q709C8"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q709C8"
FT MOD_RES 623
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q709C8"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 841
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q709C8"
FT MOD_RES 871
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 873
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1968
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 1974
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 2442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3514
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 3521
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q709C8"
FT MOD_RES 3533
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q709C8"
FT VAR_SEQ 763..802
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052246"
FT VAR_SEQ 3617..3623
FT /note="NHIKKLE -> QEMGTQE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_052247"
FT VAR_SEQ 3624..3748
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_052248"
FT CONFLICT 1759
FT /note="A -> S (in Ref. 2; BAC33809)"
FT /evidence="ECO:0000305"
FT CONFLICT 2868
FT /note="T -> P (in Ref. 3; BAC98296)"
FT /evidence="ECO:0000305"
FT CONFLICT 2916
FT /note="R -> G (in Ref. 3; BAC98296)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3748 AA; 420089 MW; 57F0943B89B7A087 CRC64;
MVLESVVADL LNRFLGDYVE NLNKSQLKLG IWGGNVALDN LQIKENALSE LDVPFKVKAG
QIDKLTLKIP WKNLYGEAVV ATLEGLYLLV VPGASIKYDA EKEEKSLQDI KQKELCRIEE
ALQKAAEKGA HSGEFMYGLE NLLYKDVKPG RKRKKHKKHF KKRFKGLDRS KDKPKEAKKD
TFLEKLATQV IKNVQVKITD IHIKYEDDIT DPERPLSFGV TLREFSLLTT NEHWTPCILN
EAEKIIYKLV KLDSLSAYWN VGCCMSYRGS REHILEQLKR EILTSTNIPP DHQYIFQPIS
ASAKLYMNPG AESELKTPKL DGNVEVQNIA IELTKPQYLS MIDFLESLDY MVRNAPYRKY
KPCLPLHTNC RQWWKYAIDS VLEVHIRRYT QPWSWSNIKN HRQLLKSYKM AYKTKLTQAK
VSEEIQKQIQ DLEKSLDVFN IILVRQQAQV EVIHSGQKLR KKSAEAGEKR GWFSGFWGKK
ESKKRDEESS VPETIDDLMT PEEKDKLFTA IGYSENAYNL ALPKQYVAHI LTLKLVSTSI
IIRENRNVPE ILRVQIIGLG TQVSQRPGAQ ALKIEAKLEH WYVTGLRQQD IVPSLVASIG
DTTSSLLKIE FETNPENSPA DQTLIVQSQP VEVIYDAKTI NAVVEFFQSN KGLDLEQITS
ATLMKLEEIK ERTATGLTHI IETRKVLDLR INLKPSYLII PQTGFHHEKS NLLILDFGTF
QLNSKDQGAQ KTANASLEEI IDKAYDKFDV EIRSVQLLFA KAEENWKKCR FQHPSTMHIL
QPMDIHVELA KAMVEKDVRM AKFKVSGGLP LMHVRISDQK IKDALCLINS IPLPQKSSTP
SPERQVASIP VLSGGTKALL GTSLLLDGVE SESDEEFFDA EDGDSQAART VKASELKKAA
EVPNEELVSL LLKFEIKEVV LELTKQQKEE ETILVFNVTQ LGTEATMRTF DLTAVSYLRK
ISLDYHDIKG SRKKPIHLIS SSDRPGLDLL KVEYIKVDRN GPSFQTTFEK TEQTVKVAFS
SLNLLLQTQA LLSSLNYLTT VIPSDSQNTG VAKEVQAMPE KQKNSPLQKV MVPSRDSDVI
GFRLFAKLNA FCVTVCDEKS NIAEIKIQGL DSSLSLQSKK QSLFARLENI IVTDVDPKTI
HKKAVSIVGN EVFRFNLDLY PDATEGDSYT DMSTVDGVVA LHVGCIQIVY LHKFLMSLLS
FLNNFQVAKE ALSAATAQAA EKAATSVKDL AQRSFRVSVD IDLKAPVIVI PQSSLSTNAV
VVDLGLIRVH NRFSLVSGED TANPPVIDKM EVQLTKLKLS RTAIQPGTSH PDIQLLHPIN
LEFFVSRNLA ANWYHKVPVV EIKGRLDSMN VSLNQEDLNL LFRILAENLG EATEDLDKGK
PRIQERGETK ACREVSTPQD VHTTQGVPAA RVEETRPVDI INVLLNFEIK EVVVTLMKKA
ERKGSPFHEL KILHLGMEAK VKAHDMTAAA YLRNISMRCF HFPDSKGEPL RIVNTSDVSD
GILLKLLFIK ADSDGPDFKT IHDNTKQKLK VSFSSLDLVL HLEALLSLMD FLSSAIPSSD
SSSSEKEPEL KPLVGESRSL AIRAVPSSYE GDAFDLKITA ELNAFNIFIC DQKSNIAEIK
IHGMDASISV KPKQTDVFAR LKNIIVMNVD SLSIHKKAVS ILGDEVFRFQ MSLYPDATEG
ENYGDMSKVD GRLSLKVGCI QIVYVHKFFM SLLSFLNNFQ AAKEALSTAT VQAAERAASS
VKDLAQKSFR LLMDIDLKAP VITIPQSSVS PNVVIADLGL IRVENKFSLV SVEQLALPPV
ADEMSIQLTQ LKLARTVLQA DSPQHDVEIL KPVNMLLCIQ RNLSAAWYTQ IPGMEIKGEL
KPMQVALSQD DLTVLMKILL ENLGEASSQP SPTQYAQEAA RVKRDTRSGP DYLKEQELAD
PKPPGDQTVT LQFDFHFDSL SIILYNSDSS QEPRLSFHND SFRLGELTLH LMASAGKMFK
DGSMNVSLKL KTCTLDDLRE GIERATSRMI DKKNDQDNNS SMIDISYSQD KNGSQVDAVL
DKLYVCASVE FLMTVADFFI KAMPQSPENI AKEIQIPSRQ TAAGRVKMEK DDSVRPNMTL
KAMITDPEVV FVASLTKADA PALTASFQCN LSLSTSKLEQ MMEASVRDLK VLACPFLRER
RGKSITTVLQ PCSLFMEKCT WASGKQNINI VVKEFVIKIS PIILNTVMTI MAAMSPKTKE
DEWKDTPKET DNLWAVKSIT DYNSWFLGVD MATEVTENFR DSEHPSIEEN CVVAVESVQV
TLECGLGHRT VPLLLAESKF SGNIKNWTSL MAAAADMTLE VHYYNETHAV WEPLIERVEG
NKPWSLKLNV KKNPIQDKSL MPGDDFIPEP QTAVHISSGA TMNITISKSC LNVFSNLAKG
FSEGAASTFD YSLKDRAPFT VKNALGVPMK VQPNRNLKVM GSPEKSDIYD VGAGQHLELD
YASLEPSRQG KLSILSRQES SLFTLTFVPY GYTEVASVPV ARPGRRLYNV RNPSASHSDS
VLVQIDATEG NKVVTLRSPL QIKNHFSIAF IIYKFVKNVK LLERIGIARP EEEFHVPLDS
YRCQLYVQPA GGLEQQYTHS STYISWKEEL HRSREVRCML QCPAVEVSFL PLIVNTVALP
DELSYIGAHG EDWDPAYVIH LYPPLTLRNL LPYSLRYLLE GTAETHELAE GSSADVLHSR
ISGEIIELVL VKYLGKNWNG HFRICDTLPE FFLVCFSSDT AEVMTVDLSV HVRRIGCRME
LSVFSPYWLI NKTSRVLQYR SEEIHVKHPA DFRDIILFSF KKKNIFSKNK VQLKISTSAW
SNGFSLDTVG SYGCVKCPAT NMEYLVGVSI KMSSFNLSRV VTLTPFCTVA NKSSLDLEVG
EIASDGSIPT NKWHYVASSE CIPFWPENLS GKLCVRVVGY EGSSKPFFYN RQDNGTLLSL
EDLNGGILVD INTAEHSTVI TFSDYHEGSA PALIMNHTQW DVLTYKQSGS QEELVLLPGE
TRLFAWADPT GIRKLTWNYA ANFGEHDLLK DECGQFPYDA NIQIHWVSFL DGRQRVLLFT
DDVALVSKAL QAEEMEQADH EVALSLHSLG LSLVNNENKQ EVSYVGITSS GVVWEMKPKQ
KWKPFSQKQI MSLEQAYSKR LASQDRGWVK LDSNFEVNFD KVPMEMRLPI RCPIKRDFLS
GIQVEFKQSP HQRSLRARLY WLQVDNQLPG TMFPVVFHPV APPKSIALDS EPKPFIDVSV
ITRFNEYSKV LQFKYFMVLI QEMALKVDQG FLGAVISLFT PTTDPEAERK RTKLIQQDID
ALNTELMESS MTDMSILSFF EHFHISPVKL HLSLSLGSGG EESDKEKQEM IAIHSVNLLL
KSIGATLTDV DDLIFKLAYY EIRYQFYKRD QLMWSVVRHY SEQFLKQMYV LVLGLDVLGN
PFGLIRGLSE GVEALFYEPF QGAVQGPEEF AEGLVIGVRS LVGHTVGGAA GVVSRITGSV
GKGLAAITMD KEYQQKRREE MGRQPKDFGD SLARGGKGFL RGVVGGVTGI ITKPVEGAKK
EGAAGFFKGI GKGLVGAVAR PTGGIIDMAS STFQGIQRVA ESTEEVSSLR PPRLIHEDGI
IRPYDRQESE GSDLLENHIK KLEGEAYQFH CAVPGNKRAV LMITNRRALF IKEVEILGHM
SVDWQCLFED FVCPPEVSEN LLKISVKEQG LFHKKDSANI GHLRKIYLKD PITAKRAFDA
IESAQSARQQ QKLMRQSSVK LLRPQGPS
