CCD93_HUMAN
ID CCD93_HUMAN Reviewed; 631 AA.
AC Q567U6; A8K3V7; Q4LE78; Q53TJ2; Q8TBX5; Q9H6R5; Q9NV15;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Coiled-coil domain-containing protein 93;
GN Name=CCDC93;
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].
RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R.,
RA Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long cDNAs
RT encoding large proteins by the ORF trap cloning method.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT CYS-179.
RC TISSUE=Lung, and Placenta;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS CYS-179 AND CYS-213.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-301 AND SER-305, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 FUNCTION, IDENTIFICATION IN THE CCC COMPLEX, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=25355947; DOI=10.1091/mbc.e14-06-1073;
RA Phillips-Krawczak C.A., Singla A., Starokadomskyy P., Deng Z.,
RA Osborne D.G., Li H., Dick C.J., Gomez T.S., Koenecke M., Zhang J.S.,
RA Dai H., Sifuentes-Dominguez L.F., Geng L.N., Kaufmann S.H., Hein M.Y.,
RA Wallis M., McGaughran J., Gecz J., van de Sluis B., Billadeau D.D.,
RA Burstein E.;
RT "COMMD1 is linked to the WASH complex and regulates endosomal trafficking
RT of the copper transporter ATP7A.";
RL Mol. Biol. Cell 26:91-103(2015).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP FUNCTION, INTERACTION WITH SNX17 AND SNX31, AND FUNCTION (MICROBIAL
RP INFECTION).
RX PubMed=28892079; DOI=10.1038/ncb3610;
RA McNally K.E., Faulkner R., Steinberg F., Gallon M., Ghai R., Pim D.,
RA Langton P., Pearson N., Danson C.M., Naegele H., Morris L.L., Singla A.,
RA Overlee B.L., Heesom K.J., Sessions R., Banks L., Collins B.M., Berger I.,
RA Billadeau D.D., Burstein E., Cullen P.J.;
RT "Retriever is a multiprotein complex for retromer-independent endosomal
RT cargo recycling.";
RL Nat. Cell Biol. 19:1214-1225(2017).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-315.
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).
CC -!- FUNCTION: Component of the CCC complex, which is involved in the
CC regulation of endosomal recycling of surface proteins, including
CC integrins, signaling receptor and channels. The CCC complex associates
CC with SNX17, retriever and WASH complexes to prevent lysosomal
CC degradation and promote cell surface recycling of numerous cargos such
CC as integrins ITGA5:ITGB1 (PubMed:28892079, PubMed:25355947). Involved
CC in copper-dependent ATP7A trafficking between the trans-Golgi network
CC and vesicles in the cell periphery; the function is proposed to depend
CC on its association within the CCC complex and cooperation with the WASH
CC complex on early endosomes and is dependent on its interaction with
CC WASHC2C (PubMed:25355947). {ECO:0000269|PubMed:25355947,
CC ECO:0000269|PubMed:28892079}.
CC -!- FUNCTION: (Microbial infection) The CCC complex, in collaboration with
CC the heterotrimeric retriever complex, mediates the exit of human
CC papillomavirus to the cell surface. {ECO:0000269|PubMed:28892079}.
CC -!- SUBUNIT: Interacts with COMMD1, COMMD2 COMMD3, COMMD4, COMMD5, COMMD6,
CC COMMD7, COMMD8, COMMD9, COMMD10, WASHC1. Interacts directly with
CC WASHC2C (PubMed:25355947). Interacts with CCDC93; proposed to be a
CC component of the CCC (COMMD/CCDC22/CCDC93) complex which contains at
CC least COMMD1 (and possibly other COMM domain-containing proteins),
CC CCDC22 and CCDC93; in the complex interacts directly with CCDC22
CC (Probable). Interacts with VPS35L; associates with the retriever
CC complex (PubMed:25355947). Interacts with SNX17 and SNX31
CC (PubMed:28892079). {ECO:0000269|PubMed:25355947,
CC ECO:0000269|PubMed:28892079, ECO:0000305|PubMed:25355947}.
CC -!- INTERACTION:
CC Q567U6; O60826: CCDC22; NbExp=19; IntAct=EBI-1104769, EBI-3943153;
CC Q567U6; Q8N668: COMMD1; NbExp=10; IntAct=EBI-1104769, EBI-1550112;
CC Q567U6; Q9Y6G5: COMMD10; NbExp=3; IntAct=EBI-1104769, EBI-1550310;
CC Q567U6; Q86X83: COMMD2; NbExp=3; IntAct=EBI-1104769, EBI-1550220;
CC Q567U6; Q9UBI1: COMMD3; NbExp=4; IntAct=EBI-1104769, EBI-714979;
CC Q567U6; Q9H0A8: COMMD4; NbExp=2; IntAct=EBI-1104769, EBI-1550064;
CC Q567U6; Q9GZQ3: COMMD5; NbExp=2; IntAct=EBI-1104769, EBI-1550256;
CC Q567U6; Q7Z4G1: COMMD6; NbExp=3; IntAct=EBI-1104769, EBI-1550081;
CC Q567U6; Q9NX08: COMMD8; NbExp=3; IntAct=EBI-1104769, EBI-725694;
CC Q567U6; Q9P000: COMMD9; NbExp=2; IntAct=EBI-1104769, EBI-1550510;
CC Q567U6; Q641Q2: WASHC2A; NbExp=9; IntAct=EBI-1104769, EBI-2870155;
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000305|PubMed:25355947}.
CC -!- SIMILARITY: Belongs to the CCDC93 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15188.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE06075.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB209993; BAE06075.1; ALT_INIT; mRNA.
DR EMBL; AK001858; BAA91945.1; -; mRNA.
DR EMBL; AK025611; BAB15188.1; ALT_INIT; mRNA.
DR EMBL; AK290722; BAF83411.1; -; mRNA.
DR EMBL; AC009303; AAX93279.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC009404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471103; EAW95197.1; -; Genomic_DNA.
DR EMBL; BC028609; AAH28609.2; -; mRNA.
DR EMBL; BC093018; AAH93018.1; -; mRNA.
DR CCDS; CCDS2121.2; -.
DR RefSeq; NP_061917.3; NM_019044.4.
DR AlphaFoldDB; Q567U6; -.
DR SMR; Q567U6; -.
DR BioGRID; 120013; 95.
DR CORUM; Q567U6; -.
DR IntAct; Q567U6; 39.
DR MINT; Q567U6; -.
DR STRING; 9606.ENSP00000365477; -.
DR TCDB; 9.A.3.1.2; the sorting nexin27 (snx27)-retromer assembly apparatus (retromeraa) family.
DR GlyGen; Q567U6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q567U6; -.
DR PhosphoSitePlus; Q567U6; -.
DR BioMuta; CCDC93; -.
DR DMDM; 97046413; -.
DR EPD; Q567U6; -.
DR jPOST; Q567U6; -.
DR MassIVE; Q567U6; -.
DR MaxQB; Q567U6; -.
DR PaxDb; Q567U6; -.
DR PeptideAtlas; Q567U6; -.
DR PRIDE; Q567U6; -.
DR ProteomicsDB; 62566; -.
DR Antibodypedia; 33361; 242 antibodies from 20 providers.
DR DNASU; 54520; -.
DR Ensembl; ENST00000376300.7; ENSP00000365477.2; ENSG00000125633.11.
DR GeneID; 54520; -.
DR KEGG; hsa:54520; -.
DR MANE-Select; ENST00000376300.7; ENSP00000365477.2; NM_019044.5; NP_061917.3.
DR UCSC; uc002tlj.4; human.
DR CTD; 54520; -.
DR DisGeNET; 54520; -.
DR GeneCards; CCDC93; -.
DR HGNC; HGNC:25611; CCDC93.
DR HPA; ENSG00000125633; Low tissue specificity.
DR neXtProt; NX_Q567U6; -.
DR OpenTargets; ENSG00000125633; -.
DR PharmGKB; PA144596460; -.
DR VEuPathDB; HostDB:ENSG00000125633; -.
DR eggNOG; KOG2701; Eukaryota.
DR GeneTree; ENSGT00390000011294; -.
DR InParanoid; Q567U6; -.
DR OMA; QYYTLYN; -.
DR OrthoDB; 1091136at2759; -.
DR PhylomeDB; Q567U6; -.
DR TreeFam; TF323318; -.
DR PathwayCommons; Q567U6; -.
DR SignaLink; Q567U6; -.
DR BioGRID-ORCS; 54520; 40 hits in 1086 CRISPR screens.
DR ChiTaRS; CCDC93; human.
DR GeneWiki; CCDC93; -.
DR GenomeRNAi; 54520; -.
DR Pharos; Q567U6; Tdark.
DR PRO; PR:Q567U6; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q567U6; protein.
DR Bgee; ENSG00000125633; Expressed in sural nerve and 203 other tissues.
DR ExpressionAtlas; Q567U6; baseline and differential.
DR Genevisible; Q567U6; HS.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR039116; CCDC93.
DR InterPro; IPR019159; CCDC93_CC.
DR PANTHER; PTHR16441; PTHR16441; 1.
DR Pfam; PF09762; CCDC93_CC; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endosome; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..631
FT /note="Coiled-coil domain-containing protein 93"
FT /id="PRO_0000234604"
FT REGION 1..430
FT /note="Sufficient for interaction with CCDC22"
FT /evidence="ECO:0000269|PubMed:25355947"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..631
FT /note="Sufficient for interaction with WASHC2C"
FT /evidence="ECO:0000269|PubMed:25355947"
FT COILED 231..428
FT /evidence="ECO:0000255"
FT COILED 560..601
FT /evidence="ECO:0000255"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VARIANT 179
FT /note="R -> C (in dbSNP:rs33975708)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_054108"
FT VARIANT 213
FT /note="R -> C (in dbSNP:rs34095554)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_054109"
FT VARIANT 228
FT /note="P -> L (in dbSNP:rs17512204)"
FT /id="VAR_054110"
FT VARIANT 315
FT /note="H -> R (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035499"
FT VARIANT 465
FT /note="Y -> H (in dbSNP:rs17047557)"
FT /id="VAR_054111"
FT CONFLICT 39
FT /note="Y -> H (in Ref. 5; AAH28609)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="L -> P (in Ref. 2; BAA91945)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 631 AA; 73198 MW; 4E8A2C350D97002B CRC64;
MGLPRGPEGQ GLPEVETRED EEQNVKLTEI LELLVAAGYF RARIKGLSPF DKVVGGMTWC
ITTCNFDVDV DLLFQENSTI GQKIALSEKI VSVLPRMKCP HQLEPHQIQG MDFIHIFPVV
QWLVKRAIET KEEMGDYIRS YSVSQFQKTY SLPEDDDFIK RKEKAIKTVV DLSEVYKPRR
KYKRHQGAEE LLDEESRIHA TLLEYGRRYG FSRQSKMEKA EDKKTALPAG LSATEKADAH
EEDELRAAEE QRIQSLMTKM TAMANEESRL TASSVGQIVG LCSAEIKQIV SEYAEKQSEL
SAEESPEKLG TSQLHRRKVI SLNKQIAQKT KHLEELRASH TSLQARYNEA KKTLTELKTY
SEKLDKEQAA LEKIESKADP SILQNLRALV AMNENLKSQE QEFKAHCREE MTRLQQEIEN
LKAERAPRGD EKTLSSGEPP GTLTSAMTHD EDLDRRYNME KEKLYKIRLL QARRNREIAI
LHRKIDEVPS RAELIQYQKR FIELYRQISA VHKETKQFFT LYNTLDDKKV YLEKEISLLN
SIHENFSQAM ASPAARDQFL RQMEQIVEGI KQSRMKMEKK KQENKMRRDQ LNDQYLELLE
KQRLYFKTVK EFKEEGRKNE MLLSKVKAKA S
