GOGA3_HUMAN
ID GOGA3_HUMAN Reviewed; 1498 AA.
AC Q08378; A5PKX6; O43241; Q6P9C7; Q86XW3; Q8TDA9; Q8WZA3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Golgin subfamily A member 3;
DE AltName: Full=Golgi complex-associated protein of 170 kDa;
DE Short=GCP170;
DE AltName: Full=Golgin-160;
GN Name=GOLGA3;
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), PHOSPHORYLATION, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Pancreatic carcinoma;
RX PubMed=9295333; DOI=10.1074/jbc.272.38.23851;
RA Misumi Y., Sohda M., Yano A., Fujiwara T., Ikehara Y.;
RT "Molecular characterization of GCP170, a 170-kDa protein associated with
RT the cytoplasmic face of the Golgi membrane.";
RL J. Biol. Chem. 272:23851-23858(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF ASP-59; ASP-139 AND
RP ASP-311, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND CLEAVAGE BY CASPASES.
RX PubMed=10791974; DOI=10.1083/jcb.149.3.603;
RA Mancini M., Machamer C.E., Roy S., Nicholson D.W., Thornberry N.A.,
RA Casciola-Rosen L.A., Rosen A.;
RT "Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during
RT apoptosis.";
RL J. Cell Biol. 149:603-612(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Kondo M., Matsukuma S., Hirose F., Matsuda M., Yoshihara M., Misumi Y.,
RA Aida M., Ikehara M., Sutou S.;
RT "Molecular characterization of Mea-2/golgin-160/GCP170 gene encoding a
RT Golgi membrane associated protein.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-840 (ISOFORMS 1/2/3).
RC TISSUE=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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 780-1348.
RC TISSUE=Liver;
RX PubMed=8315394; DOI=10.1084/jem.178.1.49;
RA Fritzler M.J., Hamel J.C., Ochs R.L., Chan E.K.L.;
RT "Molecular characterization of two human autoantigens: unique cDNAs
RT encoding 95- and 160-kD proteins of a putative family in the Golgi
RT complex.";
RL J. Exp. Med. 178:49-62(1993).
RN [6]
RP DIMERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=12130652; DOI=10.1074/jbc.m206280200;
RA Hicks S.W., Machamer C.E.;
RT "The NH2-terminal domain of Golgin-160 contains both Golgi and nuclear
RT targeting information.";
RL J. Biol. Chem. 277:35833-35839(2002).
RN [7]
RP INTERACTION WITH GOLGA7, AND SUBCELLULAR LOCATION.
RX PubMed=14522980; DOI=10.1074/jbc.m310014200;
RA Ohta E., Misumi Y., Sohda M., Fujiwara T., Yano A., Ikehara Y.;
RT "Identification and characterization of GCP16, a novel acylated Golgi
RT protein that interacts with GCP170.";
RL J. Biol. Chem. 278:51957-51967(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [9]
RP INTERACTION WITH GOPC, TISSUE SPECIFICITY, ALTERNATIVE SPLICING (ISOFORM
RP 3), SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-121; LEU-128 AND LEU-135.
RX PubMed=15951434; DOI=10.1074/jbc.m504937200;
RA Hicks S.W., Machamer C.E.;
RT "Isoform-specific interaction of golgin-160 with the Golgi-associated
RT protein PIST.";
RL J. Biol. Chem. 280:28944-28951(2005).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272; SER-385; SER-465 AND
RP SER-1392, AND 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-389 AND SER-983, AND
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).
CC -!- FUNCTION: Golgi auto-antigen; probably involved in maintaining Golgi
CC structure.
CC -!- SUBUNIT: Homodimer. Interacts with GOLGA7. Isoform 1 interacts with
CC GOPC while isoform 3 does not. {ECO:0000269|PubMed:14522980,
CC ECO:0000269|PubMed:15951434}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, Golgi stack membrane;
CC Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Golgin-160B;
CC IsoId=Q08378-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08378-2; Sequence=VSP_007728, VSP_007729;
CC Name=3;
CC IsoId=Q08378-4; Sequence=VSP_038000, VSP_038001;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested. Expressed in
CC liver, testis, lung, heart, salivary gland and kidney.
CC {ECO:0000269|PubMed:15951434}.
CC -!- DOMAIN: Extended rod-like protein with coiled-coil domains.
CC -!- PTM: Cleaved by caspases in apoptotic cells.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35921.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH60826.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA23661.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D63997; BAA23661.1; ALT_FRAME; mRNA.
DR EMBL; AF485338; AAL93149.1; -; mRNA.
DR EMBL; AB027133; BAB71953.1; -; mRNA.
DR EMBL; BC060826; AAH60826.1; ALT_SEQ; mRNA.
DR EMBL; BC142658; AAI42659.1; -; mRNA.
DR EMBL; BC146675; AAI46676.1; -; mRNA.
DR EMBL; L06148; AAA35921.1; ALT_INIT; mRNA.
DR CCDS; CCDS53846.1; -. [Q08378-4]
DR CCDS; CCDS9281.1; -. [Q08378-1]
DR PIR; JH0820; JH0820.
DR RefSeq; NP_001166028.1; NM_001172557.1. [Q08378-4]
DR RefSeq; NP_005886.2; NM_005895.3. [Q08378-1]
DR RefSeq; XP_006719799.1; XM_006719736.3. [Q08378-1]
DR RefSeq; XP_006719800.1; XM_006719737.3. [Q08378-1]
DR AlphaFoldDB; Q08378; -.
DR SMR; Q08378; -.
DR BioGRID; 109064; 169.
DR IntAct; Q08378; 49.
DR MINT; Q08378; -.
DR STRING; 9606.ENSP00000204726; -.
DR GlyGen; Q08378; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q08378; -.
DR MetOSite; Q08378; -.
DR PhosphoSitePlus; Q08378; -.
DR BioMuta; GOLGA3; -.
DR DMDM; 32470610; -.
DR EPD; Q08378; -.
DR jPOST; Q08378; -.
DR MassIVE; Q08378; -.
DR MaxQB; Q08378; -.
DR PaxDb; Q08378; -.
DR PeptideAtlas; Q08378; -.
DR PRIDE; Q08378; -.
DR ProteomicsDB; 58601; -. [Q08378-1]
DR ProteomicsDB; 58602; -. [Q08378-2]
DR ProteomicsDB; 58603; -. [Q08378-4]
DR Antibodypedia; 32127; 201 antibodies from 32 providers.
DR DNASU; 2802; -.
DR Ensembl; ENST00000204726.9; ENSP00000204726.3; ENSG00000090615.16. [Q08378-1]
DR Ensembl; ENST00000450791.8; ENSP00000410378.2; ENSG00000090615.16. [Q08378-1]
DR Ensembl; ENST00000456883.7; ENSP00000409303.2; ENSG00000090615.16. [Q08378-2]
DR Ensembl; ENST00000545875.4; ENSP00000442603.1; ENSG00000090615.16. [Q08378-4]
DR GeneID; 2802; -.
DR KEGG; hsa:2802; -.
DR MANE-Select; ENST00000450791.8; ENSP00000410378.2; NM_001389683.1; NP_001376612.1.
DR UCSC; uc001ukz.1; human. [Q08378-1]
DR CTD; 2802; -.
DR DisGeNET; 2802; -.
DR GeneCards; GOLGA3; -.
DR HGNC; HGNC:4426; GOLGA3.
DR HPA; ENSG00000090615; Low tissue specificity.
DR MIM; 602581; gene.
DR neXtProt; NX_Q08378; -.
DR OpenTargets; ENSG00000090615; -.
DR PharmGKB; PA28807; -.
DR VEuPathDB; HostDB:ENSG00000090615; -.
DR eggNOG; ENOG502QU6P; Eukaryota.
DR GeneTree; ENSGT00950000183078; -.
DR HOGENOM; CLU_005285_1_0_1; -.
DR InParanoid; Q08378; -.
DR OMA; QDDQHAQ; -.
DR OrthoDB; 87408at2759; -.
DR PhylomeDB; Q08378; -.
DR TreeFam; TF332014; -.
DR PathwayCommons; Q08378; -.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR SignaLink; Q08378; -.
DR SIGNOR; Q08378; -.
DR BioGRID-ORCS; 2802; 14 hits in 1088 CRISPR screens.
DR ChiTaRS; GOLGA3; human.
DR GeneWiki; GOLGA3; -.
DR GenomeRNAi; 2802; -.
DR Pharos; Q08378; Tbio.
DR PRO; PR:Q08378; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q08378; protein.
DR Bgee; ENSG00000090615; Expressed in tendon of biceps brachii and 209 other tissues.
DR ExpressionAtlas; Q08378; baseline and differential.
DR Genevisible; Q08378; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0090498; C:extrinsic component of Golgi membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0007283; P:spermatogenesis; IEA:InterPro.
DR InterPro; IPR033288; Golga3.
DR PANTHER; PTHR18902:SF26; PTHR18902:SF26; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Golgi apparatus;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..1498
FT /note="Golgin subfamily A member 3"
FT /id="PRO_0000190057"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..141
FT /note="Interaction with GOPC"
FT /evidence="ECO:0000269|PubMed:15951434"
FT REGION 166..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..257
FT /note="Golgi-targeting domain"
FT REGION 216..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1376..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1440..1498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 394..1459
FT /evidence="ECO:0000255"
FT COMPBIAS 71..85
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 59..60
FT /note="Cleavage; by caspase-2"
FT SITE 139..140
FT /note="Cleavage; by caspase-3"
FT SITE 311..312
FT /note="Cleavage; by caspase-7"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55937"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 983
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1090..1134
FT /note="LQESRGFRKKIKRLEESNKKLALELEHEKGKLTGLGQSNAALREH -> VRP
FT GHLLWRQRGAGHVSPGHAATRETRRTKLHRVPSVATFGVATF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038000"
FT VAR_SEQ 1135..1498
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038001"
FT VAR_SEQ 1382..1390
FT /note="RKEPKGEAS -> VLRPASLPG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_007728"
FT VAR_SEQ 1391..1498
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_007729"
FT VARIANT 70
FT /note="G -> E (in dbSNP:rs2291256)"
FT /id="VAR_020153"
FT VARIANT 264
FT /note="P -> L (in dbSNP:rs3741486)"
FT /id="VAR_021901"
FT VARIANT 1185
FT /note="K -> R (in dbSNP:rs2291260)"
FT /id="VAR_020154"
FT MUTAGEN 59
FT /note="D->A: Abolishes cleavage by caspase-2."
FT /evidence="ECO:0000269|PubMed:10791974"
FT MUTAGEN 121
FT /note="L->A: Loss of interaction with GOPC; when associated
FT with A-128 and A-135."
FT /evidence="ECO:0000269|PubMed:15951434"
FT MUTAGEN 128
FT /note="L->A: Loss of interaction with GOPC; when associated
FT with A-121 and A-135."
FT /evidence="ECO:0000269|PubMed:15951434"
FT MUTAGEN 135
FT /note="L->A: Loss of interaction with GOPC; when associated
FT with A-121 and A-128."
FT /evidence="ECO:0000269|PubMed:15951434"
FT MUTAGEN 139
FT /note="D->A: Abolishes cleavage by caspase-3."
FT /evidence="ECO:0000269|PubMed:10791974"
FT MUTAGEN 311
FT /note="D->A: Abolishes cleavage by caspase-7."
FT /evidence="ECO:0000269|PubMed:10791974"
FT CONFLICT 159
FT /note="E -> K (in Ref. 2; AAL93149)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="L -> I (in Ref. 1; BAA23661)"
FT /evidence="ECO:0000305"
FT CONFLICT 746
FT /note="H -> R (in Ref. 2; AAL93149)"
FT /evidence="ECO:0000305"
FT CONFLICT 785
FT /note="A -> V (in Ref. 4; AAA35921)"
FT /evidence="ECO:0000305"
FT CONFLICT 932
FT /note="M -> V (in Ref. 2; AAL93149)"
FT /evidence="ECO:0000305"
FT CONFLICT 1017
FT /note="K -> R (in Ref. 2; AAL93149)"
FT /evidence="ECO:0000305"
FT CONFLICT 1281
FT /note="V -> A (in Ref. 2; AAL93149)"
FT /evidence="ECO:0000305"
FT CONFLICT 1315
FT /note="R -> W (in Ref. 2; AAL93149)"
FT /evidence="ECO:0000305"
FT CONFLICT 1443
FT /note="Q -> R (in Ref. 2; AAL93149)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1498 AA; 167355 MW; 4B95CDCFD3D64667 CRC64;
MDGASAEQDG LQEDRSHSGP SSLPEAPLKP PGPLVPPDQQ DKVQCAEVNR ASTEGESPDG
PGQGGLCQNG PTPPFPDPPS SLDPTTSPVG PDASPGVAGF HDNLRKSQGT SAEGSVRKEA
LQSLRLSLPM QETQLCSTDS PLPLEKEEQV RLQARKWLEE QLKQYRVKRQ QERSSQPATK
TRLFSTLDPE LMLNPENLPR ASTLAMTKEY SFLRTSVPRG PKVGSLGLPA HPREKKTSKS
SKIRSLADYR TEDSNAGNSG GNVPAPDSTK GSLKQNRSSA ASVVSEISLS PDTDDRLENT
SLAGDSVSEV DGNDSDSSSY SSASTRGTYG ILSKTVGTQD TPYMVNGQEI PADTLGQFPS
IKDVLQAAAA EHQDQGQEVN GEVRSRRDSI CSSVSLESSA AETQEEMLQV LKEKMRLEGQ
LEALSLEASQ ALKEKAELQA QLAALSTKLQ AQVECSHSSQ QRQDSLSSEV DTLKQSCWDL
ERAMTDLQNM LEAKNASLAS SNNDLQVAEE QYQRLMAKVE DMQRSMLSKD NTVHDLRQQM
TALQSQLQQV QLERTTLTSK LKASQAEISS LQSVRQWYQQ QLALAQEARV RLQGEMAHIQ
VGQMTQAGLL EHLKLENVSL SQQLTETQHR SMKEKGRIAA QLQGIEADML DQEAAFMQIQ
EAKTMVEEDL QRRLEEFEGE RERLQRMADS AASLEQQLEQ VKLTLLQRDQ QLEALQQEHL
DLMKQLTLTQ EALQSREQSL DALQTHYDEL QARLGELQGE AASREDTICL LQNEKIILEA
ALQAAKSGKE ELDRGARRLE EGTEETSETL EKLREELAIK SGQVEHLQQE TAALKKQMQK
IKEQFLQQKV MVEAYRRDAT SKDQLISELK ATRKRLDSEL KELRQELMQV HGEKRTAEAE
LSRLHREVAQ VRQHMADLEG HLQSAQKERD EMETHLQSLQ FDKEQMVAVT EANEALKKQI
EELQQEARKA ITEQKQKMRR LGSDLTSAQK EMKTKHKAYE NAVGILSRRL QEALAAKEAA
DAELGQLRAQ GGSSDSSLAL HERIQALEAE LQAVSHSKTL LEKELQEVIA LTSQELEESR
EKVLELEDEL QESRGFRKKI KRLEESNKKL ALELEHEKGK LTGLGQSNAA LREHNSILET
ALAKREADLV QLNLQVQAVL QRKEEEDRQM KHLVQALQAS LEKEKEKVNS LKEQVAAAKV
EAGHNRRHFK AASLELSEVK KELQAKEHLV QKLQAEADDL QIREGKHSQE IAQFQAELAE
ARAQLQLLQK QLDEQLSKQP VGNQEMENLK WEVDQKEREI QSLKQQLDLT EQQGRKELEG
LQQLLQNVKS ELEMAQEDLS MTQKDKFMLQ AKVSELKNNM KTLLQQNQQL KLDLRRGAAK
TRKEPKGEAS SSNPATPIKI PDCPVPASLL EELLRPPPAV SKEPLKNLNS CLQQLKQEMD
SLQRQMEEHA LTVHESLSSW TPLEPATASP VPPGGHAGPR GDPQRHSQSR ASKEGPGE
