TPC14_HUMAN
ID TPC14_HUMAN Reviewed; 580 AA.
AC Q8WVR3; A4D2A9; D6W5U4; Q9BQJ1; Q9BUB6; Q9NV47;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Trafficking protein particle complex subunit 14;
DE AltName: Full=Microtubule-associated protein 11 {ECO:0000303|PubMed:30715179};
GN Name=TRAPPC14 {ECO:0000312|HGNC:HGNC:25604};
GN Synonyms=C7orf43 {ECO:0000312|HGNC:HGNC:25604},
GN MAP11 {ECO:0000303|PubMed:30715179};
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Ovarian carcinoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin, and Uterus;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517; THR-541 AND SER-546, AND
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491 AND SER-517, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [8]
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 [9]
RP FUNCTION.
RX PubMed=30447097; DOI=10.1111/cas.13884;
RA Amisaki M., Tsuchiya H., Sakabe T., Fujiwara Y., Shiota G.;
RT "Identification of genes involved in the regulation of TERT in
RT hepatocellular carcinoma.";
RL Cancer Sci. 110:550-560(2019).
RN [10]
RP INVOLVEMENT IN MCPH25, VARIANT MCPH25 205-GLU--LYS-580 DEL, FUNCTION,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP ALPHA-TUBULIN.
RX PubMed=30715179; DOI=10.1093/brain/awz004;
RA Perez Y., Bar-Yaacov R., Kadir R., Wormser O., Shelef I., Birk O.S.,
RA Flusser H., Birnbaum R.Y.;
RT "Mutations in the microtubule-associated protein MAP11 (C7orf43) cause
RT microcephaly in humans and zebrafish.";
RL Brain 142:574-585(2019).
RN [11]
RP IDENTIFICATION IN THE TRAPP II COMPLEX, INTERACTION WITH RAB3IP; TRAPPC10
RP AND FBF1, SUBCELLULAR LOCATION, FUNCTION, AND SUBUNIT.
RX PubMed=31467083; DOI=10.1074/jbc.ra119.008615;
RA Cuenca A., Insinna C., Zhao H., John P., Weiss M.A., Lu Q., Walia V.,
RA Specht S., Manivannan S., Stauffer J., Peden A.A., Westlake C.J.;
RT "The C7orf43/TRAPPC14 component links the TRAPPII complex to Rabin8 for
RT preciliary vesicle tethering at the mother centriole during ciliogenesis.";
RL J. Biol. Chem. 294:15418-15434(2019).
CC -!- FUNCTION: Specific subunit of the TRAPP (transport protein particle) II
CC complex, a highly conserved vesicle tethering complex that functions in
CC late Golgi trafficking as a membrane tether (PubMed:31467083,
CC PubMed:30715179). TRAPP II complex has also GEF activity toward RAB1A
CC (By similarity). TRAPPC14 is dispensable for TRAPPII complex integrity
CC but mediates RAB3IP preciliary vesicle trafficking to the mother
CC centriole during ciliogenesis (PubMed:31467083). Modulates YAP1
CC activity as transcriptional regulator (PubMed:30447097).
CC {ECO:0000250|UniProtKB:Q3TLI0, ECO:0000269|PubMed:30447097,
CC ECO:0000269|PubMed:30715179, ECO:0000269|PubMed:31467083}.
CC -!- SUBUNIT: Component of the multisubunit TRAPP II complex, which includes
CC at least TRAPPC1, TRAPPC2, TRAPPC2L, TRAPPC3, TRAPPC4, TRAPPC5,
CC TRAPPC6A/B, TRAPPC9, TRAPPC10 and TRAPPC14. TRAPPC9, TRAPPC10 and
CC TRAPPC14 are specific subunits of the TRAPP II complex
CC (PubMed:31467083). Interacts with alpha-tubulin during mitosis
CC (PubMed:30715179). Interacts with RAB3IP (via the N-terminal region);
CC this interaction mediates RAB3IP association with the TRAPP II complex
CC (PubMed:31467083). Interacts with TRAPPC10 (PubMed:31467083). Interacts
CC with FBF1 (PubMed:31467083). {ECO:0000269|PubMed:30715179,
CC ECO:0000269|PubMed:31467083}.
CC -!- INTERACTION:
CC Q8WVR3; P21549: AGXT; NbExp=3; IntAct=EBI-719893, EBI-727098;
CC Q8WVR3; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-719893, EBI-3867333;
CC Q8WVR3; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-719893, EBI-12111050;
CC Q8WVR3; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-719893, EBI-22310682;
CC Q8WVR3; P22735: TGM1; NbExp=3; IntAct=EBI-719893, EBI-2562368;
CC Q8WVR3; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-719893, EBI-11957238;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:30715179}. Vesicle {ECO:0000269|PubMed:30715179,
CC ECO:0000269|PubMed:31467083}. Midbody {ECO:0000269|PubMed:30715179}.
CC Cytoplasm {ECO:0000269|PubMed:31467083}. Note=During mitosis, precedes
CC alpha-tubulin in gap formation of cell abscission at the midbody and is
CC co-localized with PLK1 at the edges of microtubules extensions of
CC daughter cells post cytokinesis abscission (PubMed:30715179).
CC Colocalizes with RAB3IP on preciliary vesicles (PubMed:31467083).
CC {ECO:0000269|PubMed:30715179, ECO:0000269|PubMed:31467083}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WVR3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WVR3-2; Sequence=VSP_023633, VSP_023636, VSP_023637;
CC Name=3;
CC IsoId=Q8WVR3-3; Sequence=VSP_023634, VSP_023635;
CC -!- TISSUE SPECIFICITY: Broadly expressed. High levels in brain,
CC cerebellum, testis and whole blood. {ECO:0000269|PubMed:30715179}.
CC -!- DISEASE: Microcephaly 25, primary, autosomal recessive (MCPH25)
CC [MIM:618351]: A form of microcephaly, a disease defined as a head
CC circumference more than 3 standard deviations below the age, sex and
CC ethnically matched mean. Brain weight is markedly reduced and the
CC cerebral cortex is disproportionately small. MCPH25 patients
CC additionally manifest global developmental delay, severe intellectual
CC disability with speech impairment, attention deficit-hyperactivity
CC disorder, and reduced white matter and thin corpus callosum on brain
CC imaging. {ECO:0000269|PubMed:30715179}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB66490.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL136555; CAB66490.1; ALT_FRAME; mRNA.
DR EMBL; AK001787; BAA91911.1; -; mRNA.
DR EMBL; CH236956; EAL23848.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76580.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76582.1; -; Genomic_DNA.
DR EMBL; BC002749; AAH02749.2; -; mRNA.
DR EMBL; BC015722; AAH15722.2; -; mRNA.
DR CCDS; CCDS5687.1; -. [Q8WVR3-1]
DR RefSeq; NP_060745.3; NM_018275.4. [Q8WVR3-1]
DR AlphaFoldDB; Q8WVR3; -.
DR BioGRID; 120552; 43.
DR IntAct; Q8WVR3; 20.
DR STRING; 9606.ENSP00000324741; -.
DR iPTMnet; Q8WVR3; -.
DR PhosphoSitePlus; Q8WVR3; -.
DR BioMuta; C7orf43; -.
DR DMDM; 74730883; -.
DR EPD; Q8WVR3; -.
DR jPOST; Q8WVR3; -.
DR MassIVE; Q8WVR3; -.
DR MaxQB; Q8WVR3; -.
DR PaxDb; Q8WVR3; -.
DR PeptideAtlas; Q8WVR3; -.
DR PRIDE; Q8WVR3; -.
DR ProteomicsDB; 74815; -. [Q8WVR3-1]
DR ProteomicsDB; 74816; -. [Q8WVR3-2]
DR ProteomicsDB; 74817; -. [Q8WVR3-3]
DR Antibodypedia; 16406; 90 antibodies from 17 providers.
DR DNASU; 55262; -.
DR Ensembl; ENST00000316937.8; ENSP00000324741.3; ENSG00000146826.17. [Q8WVR3-1]
DR GeneID; 55262; -.
DR KEGG; hsa:55262; -.
DR MANE-Select; ENST00000316937.8; ENSP00000324741.3; NM_018275.5; NP_060745.3.
DR UCSC; uc003utr.4; human. [Q8WVR3-1]
DR CTD; 55262; -.
DR DisGeNET; 55262; -.
DR GeneCards; TRAPPC14; -.
DR HGNC; HGNC:25604; TRAPPC14.
DR HPA; ENSG00000146826; Low tissue specificity.
DR MalaCards; TRAPPC14; -.
DR MIM; 618350; gene.
DR MIM; 618351; phenotype.
DR neXtProt; NX_Q8WVR3; -.
DR NIAGADS; ENSG00000146826; -.
DR OpenTargets; ENSG00000146826; -.
DR Orphanet; 2512; Autosomal recessive primary microcephaly.
DR VEuPathDB; HostDB:ENSG00000146826; -.
DR eggNOG; ENOG502QSBJ; Eukaryota.
DR GeneTree; ENSGT00390000014725; -.
DR HOGENOM; CLU_031637_0_0_1; -.
DR InParanoid; Q8WVR3; -.
DR OMA; AHIGRRE; -.
DR OrthoDB; 536210at2759; -.
DR PhylomeDB; Q8WVR3; -.
DR TreeFam; TF331500; -.
DR PathwayCommons; Q8WVR3; -.
DR SignaLink; Q8WVR3; -.
DR BioGRID-ORCS; 55262; 18 hits in 1067 CRISPR screens.
DR ChiTaRS; C7orf43; human.
DR GeneWiki; C7orf43; -.
DR GenomeRNAi; 55262; -.
DR Pharos; Q8WVR3; Tdark.
DR PRO; PR:Q8WVR3; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8WVR3; protein.
DR Bgee; ENSG00000146826; Expressed in mucosa of transverse colon and 176 other tissues.
DR ExpressionAtlas; Q8WVR3; baseline and differential.
DR Genevisible; Q8WVR3; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:1990071; C:TRAPPII protein complex; IMP:UniProtKB.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IDA:UniProtKB.
DR InterPro; IPR031626; TRAPPC14.
DR PANTHER; PTHR16096; PTHR16096; 1.
DR Pfam; PF15806; DUF4707; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Disease variant; Phosphoprotein; Primary microcephaly;
KW Reference proteome.
FT CHAIN 1..580
FT /note="Trafficking protein particle complex subunit 14"
FT /id="PRO_0000280344"
FT REGION 90..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 541
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..378
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023633"
FT VAR_SEQ 1..374
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_023634"
FT VAR_SEQ 375..413
FT /note="SCKSPVRTYERFTVTYTLLNNLQDFLAVRLVWTPEHAQA -> MHRLFTPQS
FT GFENQMRLCWRRPCGNEERCSVCWSLFLPP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_023635"
FT VAR_SEQ 379..413
FT /note="PVRTYERFTVTYTLLNNLQDFLAVRLVWTPEHAQA -> MHRLSGFENQMRL
FT CWRRPCGNEERCSVCWSLFLPP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023636"
FT VAR_SEQ 466..468
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023637"
FT VARIANT 205..580
FT /note="Missing (in MCPH25)"
FT /evidence="ECO:0000269|PubMed:30715179"
FT /id="VAR_081463"
FT VARIANT 295
FT /note="R -> H (in dbSNP:rs2293477)"
FT /id="VAR_050817"
FT CONFLICT 497
FT /note="S -> R (in Ref. 1; CAB66490)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 580 AA; 62597 MW; EF0E23FEFB98D328 CRC64;
MESQCDYSMY FPAVPLPPRA ELAGDPGRYR ALPRRNHLYL GETVRFLLVL RCRGGAGSGT
GGGPGLGSRG AWAELATALA ALASVSAGGG MPGGGGAGDQ DSEPPGGGDP GGGGLFRGCS
PLLTHGPGPA TSGGATTLPV EEPIVSTDEV IFPLTVSLDR LPPGTPKAKI VVTVWKREIE
APEVRDQGYL RLLQTRSPGE TFRGEQSAFK AQVSTLLTLL PPPVLRCRQF TVAGKHLTVL
KVLNSSSQEE ISIWDIRILP NFNASYLPVM PDGSVLLVDN VCHQSGEVSM GSFCRLPGTS
GCFPCPLNAL EEHNFLFQLR GGEQPPPGAK EGLEVPLIAV VQWSTPKLPF TQSIYTHYRL
PSVRLDRPCF VMTASCKSPV RTYERFTVTY TLLNNLQDFL AVRLVWTPEH AQAGKQLCEE
ERRAMQAALD SVVCHTPLNN LGFSRKGSAL TFSVAFQALR TGLFELSQHM KLKLQFTASV
SHPPPEARPL SRKSSPSSPA VRDLVERHQA SLGRSQSFSH QQPSRSHLMR SGSVMERRAI
TPPVASPVGR PLYLPPDKAV LSLDKIAKRE CKVLVVEPVK
