COPG1_HUMAN
ID COPG1_HUMAN Reviewed; 874 AA.
AC Q9Y678; A8K6M8; B3KMF6; Q54AC4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Coatomer subunit gamma-1;
DE AltName: Full=Gamma-1-coat protein;
DE Short=Gamma-1-COP;
GN Name=COPG1; Synonyms=COPG;
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], INTERACTION WITH COPB1 AND TMED10, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11056392; DOI=10.1093/oxfordjournals.jbchem.a022817;
RA Futatsumori M., Kasai K., Takatsu H., Shin H.-W., Nakayama K.;
RT "Identification and characterization of novel isoforms of COP I subunits.";
RL J. Biochem. 128:793-801(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Teratocarcinoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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].
RC TISSUE=Skin;
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 FUNCTION, AND INTERACTION WITH EGFR.
RX PubMed=20674546; DOI=10.1016/j.bbrc.2010.07.096;
RA Wang Y.N., Wang H., Yamaguchi H., Lee H.J., Lee H.H., Hung M.C.;
RT "COPI-mediated retrograde trafficking from the Golgi to the ER regulates
RT EGFR nuclear transport.";
RL Biochem. Biophys. Res. Commun. 399:498-504(2010).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-594, AND IDENTIFICATION BY
RP 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 [9]
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 [10]
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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 608-874, INTERACTION WITH ZNF289,
RP AND MUTAGENESIS OF TRP-776.
RX PubMed=14690497; DOI=10.1111/j.1600-0854.2004.00158.x;
RA Watson P.J., Frigerio G., Collins B.M., Duden R., Owen D.J.;
RT "Gamma-COP appendage domain -- structure and function.";
RL Traffic 5:79-88(2004).
CC -!- FUNCTION: The coatomer is a cytosolic protein complex that binds to
CC dilysine motifs and reversibly associates with Golgi non-clathrin-
CC coated vesicles, which further mediate biosynthetic protein transport
CC from the ER, via the Golgi up to the trans Golgi network. Coatomer
CC complex is required for budding from Golgi membranes, and is essential
CC for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
CC In mammals, the coatomer can only be recruited by membranes associated
CC to ADP-ribosylation factors (ARFs), which are small GTP-binding
CC proteins; the complex also influences the Golgi structural integrity,
CC as well as the processing, activity, and endocytic recycling of LDL
CC receptors. Required for limiting lipid storage in lipid droplets.
CC Involved in lipid homeostasis by regulating the presence of perilipin
CC family members PLIN2 and PLIN3 at the lipid droplet surface and
CC promoting the association of adipocyte triglyceride lipase (PNPLA2)
CC with the lipid droplet surface to mediate lipolysis (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:20674546}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits. Interacts with
CC ZNF289/ARFGAP2 through its C-terminal appendage domain. Interacts with
CC EGFR upon EGF treatment; interaction is essential for regulation of
CC EGF-dependent nuclear transport of EGFR by retrograde trafficking from
CC the Golgi to the ER. Interacts with COPB1. Interacts with TMED10 (via
CC C-terminus). Interacts with TMED2, TMED3, TMED7 and TMED9.
CC {ECO:0000269|PubMed:11056392, ECO:0000269|PubMed:14690497,
CC ECO:0000269|PubMed:20674546}.
CC -!- INTERACTION:
CC Q9Y678; Q92538: GBF1; NbExp=2; IntAct=EBI-1049127, EBI-359050;
CC Q9Y678; Q96RS6: NUDCD1; NbExp=2; IntAct=EBI-1049127, EBI-2512429;
CC Q9Y678; Q9NTJ5: SACM1L; NbExp=3; IntAct=EBI-1049127, EBI-3917235;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11056392}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:11056392}; Peripheral membrane
CC protein {ECO:0000269|PubMed:11056392}; Cytoplasmic side
CC {ECO:0000269|PubMed:11056392}. Cytoplasmic vesicle, COPI-coated vesicle
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or
CC polymerized on the cytoplasmic side of the Golgi, as well as on the
CC vesicles/buds originating from it. Predominantly located in the cis-
CC Golgi apparatus. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the COPG family. {ECO:0000305}.
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DR EMBL; AB047846; BAB17657.1; -; mRNA.
DR EMBL; AF100756; AAD43020.1; -; mRNA.
DR EMBL; AK001724; BAG50968.1; -; mRNA.
DR EMBL; AK291693; BAF84382.1; -; mRNA.
DR EMBL; CH471052; EAW79267.1; -; Genomic_DNA.
DR EMBL; BC066650; AAH66650.1; -; mRNA.
DR CCDS; CCDS33851.1; -.
DR RefSeq; NP_057212.1; NM_016128.3.
DR PDB; 1R4X; X-ray; 1.90 A; A=608-874.
DR PDBsum; 1R4X; -.
DR AlphaFoldDB; Q9Y678; -.
DR SMR; Q9Y678; -.
DR BioGRID; 116496; 168.
DR DIP; DIP-29872N; -.
DR IntAct; Q9Y678; 68.
DR MINT; Q9Y678; -.
DR STRING; 9606.ENSP00000325002; -.
DR DrugBank; DB03963; S-(Dimethylarsenic)Cysteine.
DR GlyGen; Q9Y678; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y678; -.
DR MetOSite; Q9Y678; -.
DR PhosphoSitePlus; Q9Y678; -.
DR SwissPalm; Q9Y678; -.
DR BioMuta; COPG1; -.
DR DMDM; 12229771; -.
DR EPD; Q9Y678; -.
DR jPOST; Q9Y678; -.
DR MassIVE; Q9Y678; -.
DR MaxQB; Q9Y678; -.
DR PaxDb; Q9Y678; -.
DR PeptideAtlas; Q9Y678; -.
DR PRIDE; Q9Y678; -.
DR ProteomicsDB; 86615; -.
DR Antibodypedia; 46660; 150 antibodies from 26 providers.
DR DNASU; 22820; -.
DR Ensembl; ENST00000314797.10; ENSP00000325002.6; ENSG00000181789.14.
DR GeneID; 22820; -.
DR KEGG; hsa:22820; -.
DR MANE-Select; ENST00000314797.10; ENSP00000325002.6; NM_016128.4; NP_057212.1.
DR UCSC; uc003els.4; human.
DR CTD; 22820; -.
DR DisGeNET; 22820; -.
DR GeneCards; COPG1; -.
DR HGNC; HGNC:2236; COPG1.
DR HPA; ENSG00000181789; Low tissue specificity.
DR MIM; 615525; gene.
DR neXtProt; NX_Q9Y678; -.
DR OpenTargets; ENSG00000181789; -.
DR PharmGKB; PA26752; -.
DR VEuPathDB; HostDB:ENSG00000181789; -.
DR eggNOG; KOG1078; Eukaryota.
DR GeneTree; ENSGT00390000016313; -.
DR HOGENOM; CLU_010353_2_0_1; -.
DR InParanoid; Q9Y678; -.
DR OMA; RTIVECM; -.
DR OrthoDB; 164866at2759; -.
DR PhylomeDB; Q9Y678; -.
DR TreeFam; TF300324; -.
DR PathwayCommons; Q9Y678; -.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; Q9Y678; -.
DR BioGRID-ORCS; 22820; 662 hits in 1086 CRISPR screens.
DR ChiTaRS; COPG1; human.
DR EvolutionaryTrace; Q9Y678; -.
DR GeneWiki; COPG; -.
DR GenomeRNAi; 22820; -.
DR Pharos; Q9Y678; Tbio.
DR PRO; PR:Q9Y678; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y678; protein.
DR Bgee; ENSG00000181789; Expressed in stromal cell of endometrium and 194 other tissues.
DR ExpressionAtlas; Q9Y678; baseline and differential.
DR Genevisible; Q9Y678; HS.
DR GO; GO:0030126; C:COPI vesicle coat; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; ISS:BHF-UCL.
DR GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0051683; P:establishment of Golgi localization; ISS:BHF-UCL.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0072384; P:organelle transport along microtubule; ISS:BHF-UCL.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 2.
DR Gene3D; 2.60.40.1480; -; 1.
DR Gene3D; 3.30.310.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR032154; Coatomer_g_Cpla.
DR InterPro; IPR017106; Coatomer_gsu.
DR InterPro; IPR013040; Coatomer_gsu_app_Ig-like_dom.
DR InterPro; IPR037067; Coatomer_gsu_app_sf.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR10261; PTHR10261; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF16381; Coatomer_g_Cpla; 1.
DR Pfam; PF08752; COP-gamma_platf; 1.
DR PIRSF; PIRSF037093; Coatomer_gamma_subunit; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR SUPFAM; SSF55711; SSF55711; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..874
FT /note="Coatomer subunit gamma-1"
FT /id="PRO_0000193858"
FT REPEAT 64..101
FT /note="HEAT 1"
FT REPEAT 283..320
FT /note="HEAT 2"
FT REPEAT 322..355
FT /note="HEAT 3"
FT REPEAT 356..392
FT /note="HEAT 4"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..874
FT /note="Interaction with ZNF289/ARFGAP2"
FT /evidence="ECO:0000269|PubMed:14690497"
FT MOD_RES 594
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 681
FT /note="M -> T (in dbSNP:rs15648)"
FT /id="VAR_054039"
FT MUTAGEN 776
FT /note="W->S: Loss of interaction with ZNF289/ARFGAP2."
FT /evidence="ECO:0000269|PubMed:14690497"
FT CONFLICT 622
FT /note="E -> V (in Ref. 3; BAG50968)"
FT /evidence="ECO:0000305"
FT CONFLICT 786
FT /note="E -> G (in Ref. 3; BAG50968)"
FT /evidence="ECO:0000305"
FT CONFLICT 842
FT /note="V -> M (in Ref. 3; BAG50968)"
FT /evidence="ECO:0000305"
FT CONFLICT 854
FT /note="M -> T (in Ref. 3; BAF84382/BAG50968)"
FT /evidence="ECO:0000305"
FT HELIX 609..618
FT /evidence="ECO:0007829|PDB:1R4X"
FT HELIX 621..623
FT /evidence="ECO:0007829|PDB:1R4X"
FT STRAND 644..654
FT /evidence="ECO:0007829|PDB:1R4X"
FT STRAND 656..667
FT /evidence="ECO:0007829|PDB:1R4X"
FT STRAND 672..686
FT /evidence="ECO:0007829|PDB:1R4X"
FT STRAND 688..693
FT /evidence="ECO:0007829|PDB:1R4X"
FT STRAND 695..698
FT /evidence="ECO:0007829|PDB:1R4X"
FT STRAND 704..711
FT /evidence="ECO:0007829|PDB:1R4X"
FT STRAND 714..716
FT /evidence="ECO:0007829|PDB:1R4X"
FT STRAND 722..735
FT /evidence="ECO:0007829|PDB:1R4X"
FT TURN 737..739
FT /evidence="ECO:0007829|PDB:1R4X"
FT STRAND 747..752
FT /evidence="ECO:0007829|PDB:1R4X"
FT STRAND 756..758
FT /evidence="ECO:0007829|PDB:1R4X"
FT HELIX 760..763
FT /evidence="ECO:0007829|PDB:1R4X"
FT STRAND 764..766
FT /evidence="ECO:0007829|PDB:1R4X"
FT HELIX 772..779
FT /evidence="ECO:0007829|PDB:1R4X"
FT STRAND 785..791
FT /evidence="ECO:0007829|PDB:1R4X"
FT HELIX 797..808
FT /evidence="ECO:0007829|PDB:1R4X"
FT TURN 814..817
FT /evidence="ECO:0007829|PDB:1R4X"
FT STRAND 824..834
FT /evidence="ECO:0007829|PDB:1R4X"
FT TURN 835..837
FT /evidence="ECO:0007829|PDB:1R4X"
FT STRAND 838..862
FT /evidence="ECO:0007829|PDB:1R4X"
FT HELIX 863..872
FT /evidence="ECO:0007829|PDB:1R4X"
SQ SEQUENCE 874 AA; 97718 MW; A2FAB492C598EC98 CRC64;
MLKKFDKKDE ESGGGSNPFQ HLEKSAVLQE ARVFNETPIN PRKCAHILTK ILYLINQGEH
LGTTEATEAF FAMTKLFQSN DPTLRRMCYL TIKEMSCIAE DVIIVTSSLT KDMTGKEDNY
RGPAVRALCQ ITDSTMLQAI ERYMKQAIVD KVPSVSSSAL VSSLHLLKCS FDVVKRWVNE
AQEAASSDNI MVQYHALGLL YHVRKNDRLA VNKMISKVTR HGLKSPFAYC MMIRVASKQL
EEEDGSRDSP LFDFIESCLR NKHEMVVYEA ASAIVNLPGC SAKELAPAVS VLQLFCSSPK
AALRYAAVRT LNKVAMKHPS AVTACNLDLE NLVTDSNRSI ATLAITTLLK TGSESSIDRL
MKQISSFMSE ISDEFKVVVV QAISALCQKY PRKHAVLMNF LFTMLREEGG FEYKRAIVDC
IISIIEENSE SKETGLSHLC EFIEDCEFTV LATRILHLLG QEGPKTTNPS KYIRFIYNRV
VLEHEEVRAG AVSALAKFGA QNEEMLPSIL VLLKRCVMDD DNEVRDRATF YLNVLEQKQK
ALNAGYILNG LTVSIPGLER ALQQYTLEPS EKPFDLKSVP LATAPMAEQR TESTPITAVK
QPEKVAATRQ EIFQEQLAAV PEFRGLGPLF KSSPEPVALT ESETEYVIRC TKHTFTNHMV
FQFDCTNTLN DQTLENVTVQ MEPTEAYEVL CYVPARSLPY NQPGTCYTLV ALPKEDPTAV
ACTFSCMMKF TVKDCDPTTG ETDDEGYEDE YVLEDLEVTV ADHIQKVMKL NFEAAWDEVG
DEFEKEETFT LSTIKTLEEA VGNIVKFLGM HPCERSDKVP DNKNTHTLLL AGVFRGGHDI
LVRSRLLLLD TVTMQVTARS LEELPVDIIL ASVG
