CCD22_HUMAN
ID CCD22_HUMAN Reviewed; 627 AA.
AC O60826; A8K7G1;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Coiled-coil domain-containing protein 22;
GN Name=CCDC22; Synonyms=CXorf37; ORFNames=JM1;
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].
RC TISSUE=Peripheral blood leukocyte;
RA Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A.,
RA Meindl A.;
RT "Transcription map in Xp11.23.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
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 MRNA].
RC TISSUE=Pancreas, and Placenta;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [5]
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 [6]
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 [7]
RP INVOLVEMENT IN RTSC2, AND VARIANT RTSC2 CYS-557.
RX PubMed=24916641; DOI=10.1038/ejhg.2014.109;
RA Kolanczyk M., Krawitz P., Hecht J., Hupalowska A., Miaczynska M.,
RA Marschner K., Schlack C., Emmerich D., Kobus K., Kornak U., Robinson P.N.,
RA Plecko B., Grangl G., Uhrig S., Mundlos S., Horn D.;
RT "Missense variant in CCDC22 causes X-linked recessive intellectual
RT disability with features of Ritscher-Schinzel/3C syndrome.";
RL Eur. J. Hum. Genet. 23:633-638(2015).
RN [8]
RP INVOLVEMENT IN RTSC2, VARIANT RTSC2 ALA-17, AND TISSUE SPECIFICITY.
RX PubMed=21826058; DOI=10.1038/mp.2011.95;
RA Voineagu I., Huang L., Winden K., Lazaro M., Haan E., Nelson J.,
RA McGaughran J., Nguyen L.S., Friend K., Hackett A., Field M., Gecz J.,
RA Geschwind D.;
RT "CCDC22: a novel candidate gene for syndromic X-linked intellectual
RT disability.";
RL Mol. Psychiatry 17:4-7(2012).
RN [9]
RP FUNCTION, SUBUNIT, AND CHARACTERIZATION OF VARIANT RTSC2 ALA-17.
RX PubMed=23563313; DOI=10.1172/jci66466;
RA Starokadomskyy P., Gluck N., Li H., Chen B., Wallis M., Maine G.N., Mao X.,
RA Zaidi I.W., Hein M.Y., McDonald F.J., Lenzner S., Zecha A., Ropers H.H.,
RA Kuss A.W., McGaughran J., Gecz J., Burstein E.;
RT "CCDC22 deficiency in humans blunts activation of proinflammatory NF-kappaB
RT signaling.";
RL J. Clin. Invest. 123:2244-2256(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 CCDC93; COMMD1; COMMD2; COMMD8; COMMD9; SNX17;
RP SNX31 AND VPS35L, SUBCELLULAR LOCATION, AND FUNCTION (MICROBIAL 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 ASN-546.
RX PubMed=23092983; DOI=10.1038/tp.2012.102;
RA Nava C., Lamari F., Heron D., Mignot C., Rastetter A., Keren B., Cohen D.,
RA Faudet A., Bouteiller D., Gilleron M., Jacquette A., Whalen S., Afenjar A.,
RA Perisse D., Laurent C., Dupuits C., Gautier C., Gerard M., Huguet G.,
RA Caillet S., Leheup B., Leboyer M., Gillberg C., Delorme R., Bourgeron T.,
RA Brice A., Depienne C.;
RT "Analysis of the chromosome X exome in patients with autism spectrum
RT disorders identified novel candidate genes, including TMLHE.";
RL Transl. Psychiatry 2:E179-E179(2012).
CC -!- FUNCTION: Involved in regulation of NF-kappa-B signaling. Promotes
CC ubiquitination of I-kappa-B-kinase subunit IKBKB and its subsequent
CC proteasomal degradation leading to NF-kappa-B activation; the function
CC may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin
CC ligase complex. May down-regulate NF-kappa-B activity via association
CC with COMMD1 and involving a CUL2-dependent E3 ubiquitin ligase complex.
CC Regulates the cellular localization of COMM domain-containing proteins,
CC such as COMMD1 and COMMD10 (PubMed:23563313). Component of the CCC
CC complex, which is involved in the regulation of endosomal recycling of
CC surface proteins, including integrins, signaling receptor and channels.
CC The CCC complex associates with SNX17, retriever and WASH complexes to
CC prevent lysosomal degradation and promote cell surface recycling of
CC numerous cargos such as integrins ITGA5:ITGB1 (PubMed:28892079,
CC PubMed:25355947). Plays a role in copper ion homeostasis. Involved in
CC copper-dependent ATP7A trafficking between the trans-Golgi network and
CC vesicles in the cell periphery; the function is proposed to depend on
CC its association within the CCC complex and cooperation with the WASH
CC complex on early endosomes (PubMed:25355947).
CC {ECO:0000269|PubMed:23563313, 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 CPNE1 and CPNE4 (By similarity). Interacts with
CC COMMD1, COMMD2 COMMD3, COMMD4, COMMD5, COMMD6, COMMD7, COMMD8, COMMD9,
CC COMMD10 (PubMed:25355947). Interacts with CUL1, CUL2, CUL3, SKP1, BTRC
CC (PubMed:23563313). Interacts with CCDC93; proposed to be a component of
CC the CCC (COMMD/CCDC22/CCDC93) complex which contains at least COMMD1
CC (and possibly other COMM domain-containing proteins), CCDC22 and
CC CCDC93; in the complex interacts directly with CCDC93
CC (PubMed:25355947). Interacts with VPS35L; associates with the retriever
CC complex (PubMed:25355947, PubMed:28892079). Interacts with SNX17 and
CC SNX31 (PubMed:28892079). {ECO:0000250|UniProtKB:Q9JIG7,
CC ECO:0000269|PubMed:23563313, ECO:0000269|PubMed:25355947,
CC ECO:0000269|PubMed:28892079}.
CC -!- INTERACTION:
CC O60826; P63261: ACTG1; NbExp=3; IntAct=EBI-3943153, EBI-351292;
CC O60826; P15289: ARSA; NbExp=3; IntAct=EBI-3943153, EBI-2117357;
CC O60826; Q567U6: CCDC93; NbExp=19; IntAct=EBI-3943153, EBI-1104769;
CC O60826; Q8N668: COMMD1; NbExp=25; IntAct=EBI-3943153, EBI-1550112;
CC O60826; Q9Y6G5: COMMD10; NbExp=9; IntAct=EBI-3943153, EBI-1550310;
CC O60826; Q86X83: COMMD2; NbExp=6; IntAct=EBI-3943153, EBI-1550220;
CC O60826; Q9UBI1: COMMD3; NbExp=7; IntAct=EBI-3943153, EBI-714979;
CC O60826; Q9H0A8: COMMD4; NbExp=6; IntAct=EBI-3943153, EBI-1550064;
CC O60826; Q9GZQ3: COMMD5; NbExp=6; IntAct=EBI-3943153, EBI-1550256;
CC O60826; Q7Z4G1: COMMD6; NbExp=7; IntAct=EBI-3943153, EBI-1550081;
CC O60826; Q86VX2: COMMD7; NbExp=3; IntAct=EBI-3943153, EBI-1550280;
CC O60826; Q9NX08: COMMD8; NbExp=6; IntAct=EBI-3943153, EBI-725694;
CC O60826; Q9P000: COMMD9; NbExp=8; IntAct=EBI-3943153, EBI-1550510;
CC O60826; Q13616: CUL1; NbExp=3; IntAct=EBI-3943153, EBI-359390;
CC O60826; Q13618: CUL3; NbExp=2; IntAct=EBI-3943153, EBI-456129;
CC O60826; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-3943153, EBI-3044087;
CC O60826; O43482: OIP5; NbExp=3; IntAct=EBI-3943153, EBI-536879;
CC O60826; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-3943153, EBI-739895;
CC O60826; Q641Q2: WASHC2A; NbExp=6; IntAct=EBI-3943153, EBI-2870155;
CC O60826; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-3943153, EBI-25492395;
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000305|PubMed:28892079}.
CC -!- TISSUE SPECIFICITY: Widely expressed in adult tissues and in fetal
CC liver and brain, with highest levels in prostate and lowest in skeletal
CC muscle. {ECO:0000269|PubMed:21826058}.
CC -!- DISEASE: Ritscher-Schinzel syndrome 2 (RTSC2) [MIM:300963]: A form of
CC Ritscher-Schinzel syndrome, a developmental malformation syndrome
CC characterized by cerebellar brain malformations, congenital heart
CC defects, and craniofacial abnormalities. RTSC2 is an X-linked recessive
CC form characterized by intellectual disability associated with posterior
CC fossa defects, cardiac malformations, and minor abnormalities of the
CC face and distal extremities. {ECO:0000269|PubMed:21826058,
CC ECO:0000269|PubMed:23563313, ECO:0000269|PubMed:24916641}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the CCDC22 family. {ECO:0000305}.
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DR EMBL; AJ005890; CAA06747.1; -; mRNA.
DR EMBL; AK291976; BAF84665.1; -; mRNA.
DR EMBL; BC000972; AAH00972.1; -; mRNA.
DR EMBL; BC011675; AAH11675.1; -; mRNA.
DR CCDS; CCDS14322.1; -.
DR RefSeq; NP_054727.1; NM_014008.4.
DR AlphaFoldDB; O60826; -.
DR SMR; O60826; -.
DR BioGRID; 118780; 137.
DR CORUM; O60826; -.
DR IntAct; O60826; 76.
DR MINT; O60826; -.
DR STRING; 9606.ENSP00000365401; -.
DR TCDB; 9.A.3.1.2; the sorting nexin27 (snx27)-retromer assembly apparatus (retromeraa) family.
DR GlyGen; O60826; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O60826; -.
DR PhosphoSitePlus; O60826; -.
DR BioMuta; CCDC22; -.
DR EPD; O60826; -.
DR jPOST; O60826; -.
DR MassIVE; O60826; -.
DR MaxQB; O60826; -.
DR PaxDb; O60826; -.
DR PeptideAtlas; O60826; -.
DR PRIDE; O60826; -.
DR ProteomicsDB; 49610; -.
DR Antibodypedia; 368; 186 antibodies from 30 providers.
DR DNASU; 28952; -.
DR Ensembl; ENST00000376227.4; ENSP00000365401.3; ENSG00000101997.13.
DR GeneID; 28952; -.
DR KEGG; hsa:28952; -.
DR MANE-Select; ENST00000376227.4; ENSP00000365401.3; NM_014008.5; NP_054727.1.
DR UCSC; uc004dnd.2; human.
DR CTD; 28952; -.
DR DisGeNET; 28952; -.
DR GeneCards; CCDC22; -.
DR GeneReviews; CCDC22; -.
DR HGNC; HGNC:28909; CCDC22.
DR HPA; ENSG00000101997; Low tissue specificity.
DR MalaCards; CCDC22; -.
DR MIM; 300859; gene.
DR MIM; 300963; phenotype.
DR neXtProt; NX_O60826; -.
DR OpenTargets; ENSG00000101997; -.
DR Orphanet; 7; 3C syndrome.
DR PharmGKB; PA134947763; -.
DR VEuPathDB; HostDB:ENSG00000101997; -.
DR eggNOG; KOG1937; Eukaryota.
DR GeneTree; ENSGT00390000003809; -.
DR HOGENOM; CLU_024231_1_0_1; -.
DR InParanoid; O60826; -.
DR OMA; KFEQHIQ; -.
DR OrthoDB; 985190at2759; -.
DR PhylomeDB; O60826; -.
DR TreeFam; TF325575; -.
DR PathwayCommons; O60826; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; O60826; -.
DR BioGRID-ORCS; 28952; 30 hits in 703 CRISPR screens.
DR GenomeRNAi; 28952; -.
DR Pharos; O60826; Tbio.
DR PRO; PR:O60826; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O60826; protein.
DR Bgee; ENSG00000101997; Expressed in granulocyte and 176 other tissues.
DR ExpressionAtlas; O60826; baseline and differential.
DR Genevisible; O60826; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0097602; F:cullin family protein binding; IDA:UniProtKB.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IMP:UniProtKB.
DR GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; IMP:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:UniProtKB.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR008530; CCDC22.
DR PANTHER; PTHR15668; PTHR15668; 1.
DR Pfam; PF05667; DUF812; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Disease variant; Endosome; Intellectual disability;
KW Phosphoprotein; Protein transport; Reference proteome; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..627
FT /note="Coiled-coil domain-containing protein 22"
FT /id="PRO_0000076199"
FT REGION 1..447
FT /note="Sufficicient and required for interaction with
FT CCDC93"
FT /evidence="ECO:0000269|PubMed:25355947"
FT REGION 1..321
FT /note="Sufficient for interaction with COMMD1"
FT /evidence="ECO:0000269|PubMed:25355947"
FT REGION 218..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 447..535
FT /evidence="ECO:0000255"
FT COMPBIAS 220..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087"
FT VARIANT 17
FT /note="T -> A (in RTSC2; may affect splicing and/or have a
FT negative impact on transcription efficiency; results in
FT decreased interaction with COMMD1; dbSNP:rs863225428)"
FT /evidence="ECO:0000269|PubMed:21826058,
FT ECO:0000269|PubMed:23563313"
FT /id="VAR_065912"
FT VARIANT 546
FT /note="D -> N (in dbSNP:rs147222955)"
FT /evidence="ECO:0000269|PubMed:23092983"
FT /id="VAR_076265"
FT VARIANT 557
FT /note="Y -> C (in RTSC2; dbSNP:rs863225429)"
FT /evidence="ECO:0000269|PubMed:24916641"
FT /id="VAR_075063"
FT CONFLICT 412
FT /note="Q -> R (in Ref. 2; BAF84665)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 627 AA; 70756 MW; C3704BBCD9EA0386 CRC64;
MEEADRILIH SLRQAGTAVP PDVQTLRAFT TELVVEAVVR CLRVINPAVG SGLSPLLPLA
MSARFRLAMS LAQACMDLGY PLELGYQNFL YPSEPDLRDL LLFLAERLPT DASEDADQPA
GDSAILLRAI GSQIRDQLAL PWVPPHLRTP KLQHLQGSAL QKPFHASRLV VPELSSRGEP
REFQASPLLL PVPTQVPQPV GRVASLLEHH ALQLCQQTGR DRPGDEDWVH RTSRLPPQED
TRAQRQRLQK QLTEHLRQSW GLLGAPIQAR DLGELLQAWG AGAKTGAPKG SRFTHSEKFT
FHLEPQAQAT QVSDVPATSR RPEQVTWAAQ EQELESLREQ LEGVNRSIEE VEADMKTLGV
SFVQAESECR HSKLSTAERE QALRLKSRAV ELLPDGTANL AKLQLVVENS AQRVIHLAGQ
WEKHRVPLLA EYRHLRKLQD CRELESSRRL AEIQELHQSV RAAAEEARRK EEVYKQLMSE
LETLPRDVSR LAYTQRILEI VGNIRKQKEE ITKILSDTKE LQKEINSLSG KLDRTFAVTD
ELVFKDAKKD DAVRKAYKYL AALHENCSQL IQTIEDTGTI MREVRDLEEQ IETELGKKTL
SNLEKIREDY RALRQENAGL LGRVREA
