CCD91_HUMAN
ID CCD91_HUMAN Reviewed; 441 AA.
AC Q7Z6B0; B3KSA3; C9JR07; Q68D43; Q6IA78; Q8NEN7; Q9NUW9;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Coiled-coil domain-containing protein 91;
DE AltName: Full=GGA-binding partner;
DE AltName: Full=p56 accessory protein;
GN Name=CCDC91; Synonyms=GGABP; ORFNames=HSD8;
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] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INTERACTION WITH GGA1; GGA2 AND AP1G1, DIMERIZATION, AND
RP VARIANT MET-314.
RX PubMed=12808037; DOI=10.1091/mbc.e02-11-0735;
RA Lui W.W.Y., Collins B.M., Hirst J., Motley A., Millar C., Schu P.,
RA Owen D.J., Robinson M.S.;
RT "Binding partners for the COOH-terminal appendage domains of the GGAs and
RT gamma-adaptin.";
RL Mol. Biol. Cell 14:2385-2398(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 167-441 (ISOFORM 1), AND VARIANT MET-314.
RC TISSUE=Placenta, and Testis;
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=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT MET-314.
RC TISSUE=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 108-441 (ISOFORM 3).
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 202-441, AND VARIANT MET-314.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 202-441, AND VARIANT MET-314.
RC TISSUE=Testis;
RA Hu T.H., Miao S.Y., Zhang X.D., Qiao Y., Liang G., Wang L.F.;
RT "A new spermatogenesis-related gene.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17596511; DOI=10.1091/mbc.e07-02-0190;
RA Mardones G.A., Burgos P.V., Brooks D.A., Parkinson-Lawrence E., Mattera R.,
RA Bonifacino J.S.;
RT "The trans-Golgi network accessory protein p56 promotes long-range movement
RT of GGA/clathrin-containing transport carriers and lysosomal enzyme
RT sorting.";
RL Mol. Biol. Cell 18:3486-3501(2007).
RN [9]
RP IDENTIFICATION BY 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 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-16 IN COMPLEX WITH GGA1.
RX PubMed=12858163; DOI=10.1038/nsb955;
RA Collins B.M., Praefcke G.J., Robinson M.S., Owen D.J.;
RT "Structural basis for binding of accessory proteins by the appendage domain
RT of GGAs.";
RL Nat. Struct. Biol. 10:607-613(2003).
CC -!- FUNCTION: Involved in the regulation of membrane traffic through the
CC trans-Golgi network (TGN). Functions in close cooperation with the GGAs
CC in the sorting of hydrolases to lysosomes.
CC {ECO:0000269|PubMed:17596511}.
CC -!- SUBUNIT: Homodimer. Interacts with GGA1, GGA2 and AP1G1.
CC {ECO:0000269|PubMed:12808037, ECO:0000269|PubMed:12858163}.
CC -!- INTERACTION:
CC Q7Z6B0-2; Q16543: CDC37; NbExp=3; IntAct=EBI-12012082, EBI-295634;
CC Q7Z6B0-2; Q9UIK4: DAPK2; NbExp=3; IntAct=EBI-12012082, EBI-77154;
CC Q7Z6B0-2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-12012082, EBI-739832;
CC Q7Z6B0-2; Q6MZQ0: PRR5L; NbExp=3; IntAct=EBI-12012082, EBI-1567866;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12808037};
CC Peripheral membrane protein {ECO:0000269|PubMed:12808037}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:12808037};
CC Peripheral membrane protein {ECO:0000269|PubMed:12808037}. Golgi
CC apparatus, trans-Golgi network {ECO:0000269|PubMed:17596511}.
CC Note=Colocalizes with GGA1, GGA2 and GGA3.
CC {ECO:0000269|PubMed:12808037, ECO:0000269|PubMed:17596511}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7Z6B0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z6B0-2; Sequence=VSP_013243;
CC Name=3;
CC IsoId=Q7Z6B0-3; Sequence=VSP_013244;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12808037}.
CC -!- MISCELLANEOUS: [Isoform 1]: Binds GGAs.
CC -!- MISCELLANEOUS: [Isoform 2]: Does not bind GGAs. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91995.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY289196; AAP42284.1; -; mRNA.
DR EMBL; AK001950; BAA91995.1; ALT_INIT; mRNA.
DR EMBL; AK093152; BAG52665.1; -; mRNA.
DR EMBL; AC022079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC024939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC084754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028682; AAH28682.1; -; mRNA.
DR EMBL; CR749586; CAH18385.1; -; mRNA.
DR EMBL; CR457277; CAG33558.1; -; mRNA.
DR EMBL; AY251168; AAP20065.1; -; mRNA.
DR CCDS; CCDS81675.1; -. [Q7Z6B0-3]
DR CCDS; CCDS8716.1; -. [Q7Z6B0-1]
DR RefSeq; NP_001317296.1; NM_001330367.1. [Q7Z6B0-3]
DR RefSeq; NP_060788.3; NM_018318.4. [Q7Z6B0-1]
DR RefSeq; XP_005253471.1; XM_005253414.1. [Q7Z6B0-1]
DR RefSeq; XP_005253472.1; XM_005253415.1. [Q7Z6B0-2]
DR RefSeq; XP_006719167.1; XM_006719104.2. [Q7Z6B0-1]
DR RefSeq; XP_006719168.1; XM_006719105.1.
DR RefSeq; XP_011519031.1; XM_011520729.2.
DR RefSeq; XP_016875058.1; XM_017019569.1. [Q7Z6B0-1]
DR RefSeq; XP_016875063.1; XM_017019574.1. [Q7Z6B0-2]
DR RefSeq; XP_016875064.1; XM_017019575.1.
DR RefSeq; XP_016875065.1; XM_017019576.1.
DR PDB; 1OM9; X-ray; 2.50 A; P/Q=2-16.
DR PDBsum; 1OM9; -.
DR AlphaFoldDB; Q7Z6B0; -.
DR SMR; Q7Z6B0; -.
DR BioGRID; 120584; 29.
DR IntAct; Q7Z6B0; 17.
DR STRING; 9606.ENSP00000438040; -.
DR iPTMnet; Q7Z6B0; -.
DR PhosphoSitePlus; Q7Z6B0; -.
DR BioMuta; CCDC91; -.
DR DMDM; 296434429; -.
DR EPD; Q7Z6B0; -.
DR jPOST; Q7Z6B0; -.
DR MassIVE; Q7Z6B0; -.
DR MaxQB; Q7Z6B0; -.
DR PaxDb; Q7Z6B0; -.
DR PeptideAtlas; Q7Z6B0; -.
DR PRIDE; Q7Z6B0; -.
DR ProteomicsDB; 69389; -. [Q7Z6B0-1]
DR ProteomicsDB; 69390; -. [Q7Z6B0-2]
DR ProteomicsDB; 69391; -. [Q7Z6B0-3]
DR TopDownProteomics; Q7Z6B0-1; -. [Q7Z6B0-1]
DR Antibodypedia; 24462; 113 antibodies from 18 providers.
DR DNASU; 55297; -.
DR Ensembl; ENST00000381259.5; ENSP00000370658.1; ENSG00000123106.11. [Q7Z6B0-1]
DR Ensembl; ENST00000536442.6; ENSP00000445660.2; ENSG00000123106.11. [Q7Z6B0-1]
DR Ensembl; ENST00000539107.5; ENSP00000440513.1; ENSG00000123106.11. [Q7Z6B0-3]
DR Ensembl; ENST00000545336.5; ENSP00000438040.1; ENSG00000123106.11. [Q7Z6B0-1]
DR GeneID; 55297; -.
DR KEGG; hsa:55297; -.
DR MANE-Select; ENST00000536442.6; ENSP00000445660.2; NM_018318.5; NP_060788.3.
DR UCSC; uc001riq.4; human. [Q7Z6B0-1]
DR CTD; 55297; -.
DR DisGeNET; 55297; -.
DR GeneCards; CCDC91; -.
DR HGNC; HGNC:24855; CCDC91.
DR HPA; ENSG00000123106; Low tissue specificity.
DR MIM; 617366; gene.
DR neXtProt; NX_Q7Z6B0; -.
DR OpenTargets; ENSG00000123106; -.
DR PharmGKB; PA144596458; -.
DR VEuPathDB; HostDB:ENSG00000123106; -.
DR eggNOG; ENOG502QW5U; Eukaryota.
DR GeneTree; ENSGT00390000015899; -.
DR HOGENOM; CLU_050535_1_0_1; -.
DR InParanoid; Q7Z6B0; -.
DR OMA; QAHRCEE; -.
DR PhylomeDB; Q7Z6B0; -.
DR TreeFam; TF336441; -.
DR PathwayCommons; Q7Z6B0; -.
DR SignaLink; Q7Z6B0; -.
DR BioGRID-ORCS; 55297; 16 hits in 1080 CRISPR screens.
DR ChiTaRS; CCDC91; human.
DR EvolutionaryTrace; Q7Z6B0; -.
DR GenomeRNAi; 55297; -.
DR Pharos; Q7Z6B0; Tbio.
DR PRO; PR:Q7Z6B0; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q7Z6B0; protein.
DR Bgee; ENSG00000123106; Expressed in left testis and 196 other tissues.
DR ExpressionAtlas; Q7Z6B0; baseline and differential.
DR Genevisible; Q7Z6B0; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0090160; P:Golgi to lysosome transport; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR034592; CCDC91.
DR PANTHER; PTHR35072; PTHR35072; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..441
FT /note="Coiled-coil domain-containing protein 91"
FT /id="PRO_0000087478"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..16
FT /note="GGA1-binding motif"
FT REGION 210..413
FT /note="Homodimerization"
FT COILED 130..209
FT /evidence="ECO:0000255"
FT COILED 249..407
FT /evidence="ECO:0000255"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AY97"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AY97"
FT VAR_SEQ 1..36
FT /note="MDDDDFGGFEAAETFDGGSGETQTTSPAIPWAAFPA -> MPMWNK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_013243"
FT VAR_SEQ 219..254
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_013244"
FT VARIANT 261
FT /note="M -> V (in dbSNP:rs1133028)"
FT /id="VAR_021531"
FT VARIANT 314
FT /note="V -> M (in dbSNP:rs10771427)"
FT /evidence="ECO:0000269|PubMed:12808037,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.6, ECO:0000269|Ref.7"
FT /id="VAR_021532"
FT CONFLICT 36
FT /note="A -> T (in Ref. 1; AAP42284)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="I -> V (in Ref. 5; CAH18385)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="Q -> R (in Ref. 5; CAH18385)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="E -> D (in Ref. 6; CAG33558)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 49971 MW; E63AA5D2FB4BEDF1 CRC64;
MDDDDFGGFE AAETFDGGSG ETQTTSPAIP WAAFPAVSGV HLSPSSPEIV LDRDHSSSIG
CLSSDAIISS PENTHAANSI VSQTIPKAQI QQSTHTHLDI SLFPLGLTDE KSNGTIALVD
DSEDPGANVS NIQLQQKISS LEIKLKVSEE EKQRIKQDVE SLMEKHNVLE KGFLKEKEQE
AISFQDRYKE LQEKHKQELE DMRKAGHEAL SIIVDEYKAL LQSSVKQQVE AIEKQYISAI
EKQAHKCEEL LNAQHQRLLE MLDTEKELLK EKIKEALIQQ SQEQKEILEK CLEEERQRNK
EALVSAAKLE KEAVKDAVLK VVEEERKNLE KAHAEERELW KTEHAKDQEK VSQEIQKAIQ
EQRKISQETV KAAIIEEQKR SEKAVEEAVK RTRDELIEYI KEQKRLDQVI RQRSLSSLEL
FLSCAQKQLS ALIATEPVDI E
