COPG2_HUMAN
ID COPG2_HUMAN Reviewed; 871 AA.
AC Q9UBF2; A6NH74; Q2NLA0; Q54AC3; Q8WVW8;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Coatomer subunit gamma-2;
DE AltName: Full=Gamma-2-coat protein;
DE Short=Gamma-2-COP;
GN Name=COPG2;
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).
RA Whitney J.A., Godzich M., Kreis T.E.;
RT "Newly identified coatomer subunits reveal multiple copy complexes acting
RT in the early secretory pathway.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10556286; DOI=10.1093/hmg/8.13.2387;
RA Blagitko N., Schulz U., Schinzel A.A., Ropers H.-H., Kalscheuer V.M.;
RT "Gamma2-COP, a novel imprinted gene on chromosome 7q32, defines a new
RT imprinting cluster in the human genome.";
RL Hum. Mol. Genet. 8:2387-2396(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH TMED10.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 7-871 (ISOFORM 1).
RC TISSUE=Brain, and Eye;
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 [9]
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 [10]
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 [11]
RP INTERACTION WITH JAGN1.
RX PubMed=25129144; DOI=10.1038/ng.3069;
RA Boztug K., Jaervinen P.M., Salzer E., Racek T., Moench S., Garncarz W.,
RA Gertz E.M., Schaeffer A.A., Antonopoulos A., Haslam S.M., Schieck L.,
RA Puchalka J., Diestelhorst J., Appaswamy G., Lescoeur B., Giambruno R.,
RA Bigenzahn J.W., Elling U., Pfeifer D., Conde C.D., Albert M.H., Welte K.,
RA Brandes G., Sherkat R., van der Werff Ten Bosch J., Rezaei N., Etzioni A.,
RA Bellanne-Chantelot C., Superti-Furga G., Penninger J.M., Bennett K.L.,
RA von Blume J., Dell A., Donadieu J., Klein C.;
RT "JAGN1 deficiency causes aberrant myeloid cell homeostasis and congenital
RT neutropenia.";
RL Nat. Genet. 46:1021-1027(2014).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomeric complex. Binds to CDC42. Interacts with JAGN1.
CC Interacts with TMED10 (via cytoplasmic domain) (PubMed:11056392).
CC {ECO:0000269|PubMed:11056392, ECO:0000269|PubMed:25129144}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Golgi apparatus
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated
CC vesicle membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is
CC cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as
CC well as on the vesicles/buds originating from it. Tends to be more
CC abundant in the trans-Golgi network compared to the cis-Golgi.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UBF2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBF2-2; Sequence=VSP_055534, VSP_055535;
CC -!- SIMILARITY: Belongs to the COPG family. {ECO:0000305}.
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DR EMBL; AF207598; AAF19433.1; -; mRNA.
DR EMBL; AF157833; AAF14271.1; -; mRNA.
DR EMBL; AB047847; BAB17658.1; -; mRNA.
DR EMBL; AK291409; BAF84098.1; -; mRNA.
DR EMBL; AC090520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236950; EAL24085.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83769.1; -; Genomic_DNA.
DR EMBL; BC017443; AAH17443.2; -; mRNA.
DR EMBL; BC110796; AAI10797.1; -; mRNA.
DR CCDS; CCDS75662.1; -. [Q9UBF2-1]
DR CCDS; CCDS78275.1; -. [Q9UBF2-2]
DR RefSeq; NP_001276962.1; NM_001290033.1. [Q9UBF2-2]
DR RefSeq; NP_036265.3; NM_012133.5. [Q9UBF2-1]
DR AlphaFoldDB; Q9UBF2; -.
DR SMR; Q9UBF2; -.
DR BioGRID; 117926; 110.
DR IntAct; Q9UBF2; 38.
DR MINT; Q9UBF2; -.
DR STRING; 9606.ENSP00000402346; -.
DR GlyGen; Q9UBF2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UBF2; -.
DR MetOSite; Q9UBF2; -.
DR PhosphoSitePlus; Q9UBF2; -.
DR BioMuta; COPG2; -.
DR EPD; Q9UBF2; -.
DR jPOST; Q9UBF2; -.
DR MassIVE; Q9UBF2; -.
DR MaxQB; Q9UBF2; -.
DR PaxDb; Q9UBF2; -.
DR PeptideAtlas; Q9UBF2; -.
DR PRIDE; Q9UBF2; -.
DR ProteomicsDB; 83955; -. [Q9UBF2-1]
DR Antibodypedia; 69166; 93 antibodies from 20 providers.
DR DNASU; 26958; -.
DR Ensembl; ENST00000330992.8; ENSP00000331218.8; ENSG00000158623.14. [Q9UBF2-2]
DR Ensembl; ENST00000425248.5; ENSP00000402346.2; ENSG00000158623.14. [Q9UBF2-1]
DR GeneID; 26958; -.
DR KEGG; hsa:26958; -.
DR MANE-Select; ENST00000425248.5; ENSP00000402346.2; NM_012133.6; NP_036265.3.
DR UCSC; uc033ahl.2; human. [Q9UBF2-1]
DR CTD; 26958; -.
DR DisGeNET; 26958; -.
DR GeneCards; COPG2; -.
DR HGNC; HGNC:2237; COPG2.
DR HPA; ENSG00000158623; Low tissue specificity.
DR MIM; 604355; gene.
DR neXtProt; NX_Q9UBF2; -.
DR OpenTargets; ENSG00000158623; -.
DR PharmGKB; PA26753; -.
DR VEuPathDB; HostDB:ENSG00000158623; -.
DR eggNOG; KOG1078; Eukaryota.
DR GeneTree; ENSGT00390000016313; -.
DR HOGENOM; CLU_010353_2_0_1; -.
DR InParanoid; Q9UBF2; -.
DR OMA; YMTQYHA; -.
DR PhylomeDB; Q9UBF2; -.
DR PathwayCommons; Q9UBF2; -.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; Q9UBF2; -.
DR BioGRID-ORCS; 26958; 6 hits in 252 CRISPR screens.
DR ChiTaRS; COPG2; human.
DR GeneWiki; COPG2; -.
DR GenomeRNAi; 26958; -.
DR Pharos; Q9UBF2; Tbio.
DR PRO; PR:Q9UBF2; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UBF2; protein.
DR Bgee; ENSG00000158623; Expressed in cortical plate and 133 other tissues.
DR ExpressionAtlas; Q9UBF2; baseline and differential.
DR Genevisible; Q9UBF2; HS.
DR GO; GO:0030126; C:COPI vesicle coat; IDA: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:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
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:0006891; P:intra-Golgi vesicle-mediated transport; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0072384; P:organelle transport along microtubule; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; TAS:UniProtKB.
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 Alternative splicing; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..871
FT /note="Coatomer subunit gamma-2"
FT /id="PRO_0000193862"
FT REPEAT 64..101
FT /note="HEAT 1"
FT REPEAT 283..320
FT /note="HEAT 2"
FT REPEAT 321..355
FT /note="HEAT 3"
FT REPEAT 356..392
FT /note="HEAT 4"
FT REPEAT 395..430
FT /note="HEAT 5"
FT REPEAT 467..504
FT /note="HEAT 6"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 594
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y678"
FT VAR_SEQ 717..726
FT /note="VAGSFSCTMK -> GTNPQKGGDT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055534"
FT VAR_SEQ 727..871
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055535"
FT VARIANT 547
FT /note="I -> L (in dbSNP:rs10128)"
FT /id="VAR_060181"
FT VARIANT 626
FT /note="P -> L (in dbSNP:rs17333054)"
FT /id="VAR_060182"
SQ SEQUENCE 871 AA; 97622 MW; D361A0E74069CBEB CRC64;
MIKKFDKKDE ESGSGSNPFQ HLEKSAVLQE ARIFNETPIN PRRCLHILTK ILYLLNQGEH
FGTTEATEAF FAMTRLFQSN DQTLRRMCYL TIKEMATISE DVIIVTSSLT KDMTGKEDVY
RGPAIRALCR ITDGTMLQAI ERYMKQAIVD KVSSVSSSAL VSSLHMMKIS YDVVKRWINE
AQEAASSDNI MVQYHALGVL YHLRKNDRLA VSKMLNKFTK SGLKSQFAYC MLIRIASRLL
KETEDGHESP LFDFIESCLR NKHEMVIYEA ASAIIHLPNC TARELAPAVS VLQLFCSSPK
PALRYAAVRT LNKVAMKHPS AVTACNLDLE NLITDSNRSI ATLAITTLLK TGSESSVDRL
MKQISSFVSE ISDEFKVVVV QAISALCQKY PRKHSVMMTF LSNMLRDDGG FEYKRAIVDC
IISIVEENPE SKEAGLAHLC EFIEDCEHTV LATKILHLLG KEGPRTPVPS KYIRFIFNRV
VLENEAVRAA AVSALAKFGA QNESLLPSIL VLLQRCMMDT DDEVRDRATF YLNVLQQRQM
ALNATYIFNG LTVSVPGMEK ALHQYTLEPS EKPFDMKSIP LAMAPVFEQK AEITLVATKP
EKLAPSRQDI FQEQLAAIPE FLNIGPLFKS SEPVQLTEAE TEYFVRCIKH MFTNHIVFQF
DCTNTLNDQL LEKVTVQMEP SDSYEVLSCI PAPSLPYNQP GICYTLVRLP DDDPTAVAGS
FSCTMKFTVR DCDPNTGVPD EDGYDDEYVL EDLEVTVSDH IQKVLKPNFA AAWEEVGDTF
EKEETFALSS TKTLEEAVNN IITFLGMQPC ERSDKVPENK NSHSLYLAGI FRGGYDLLVR
SRLALADGVT MQVTVRSKER TPVDVILASV G
