STAG3_HUMAN
ID STAG3_HUMAN Reviewed; 1225 AA.
AC Q9UJ98; A6H8Z1; B4DZ10; D6W5U8; H7BYK9; Q8NDP3;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Cohesin subunit SA-3;
DE AltName: Full=SCC3 homolog 3;
DE AltName: Full=Stromal antigen 3;
DE AltName: Full=Stromalin-3;
GN Name=STAG3;
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), AND CHARACTERIZATION.
RC TISSUE=Testis;
RX PubMed=10698974; DOI=10.1096/fasebj.14.3.581;
RA Pezzi N., Prieto I., Kremer L., Perez Jurado L.A., Valero C., Del Mazo J.,
RA Martinez-A C., Barbero J.L.;
RT "STAG3, a novel gene encoding a protein involved in meiotic chromosome
RT pairing and location of STAG3-related genes flanking the Williams-Beuren
RT syndrome deletion.";
RL FASEB J. 14:581-592(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=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 [4]
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 [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP SUBCELLULAR LOCATION DURING MEIOSIS.
RX PubMed=12034751; DOI=10.1093/embo-reports/kvf108;
RA Prieto I., Pezzi N., Buesa J.M., Kremer L., Barthelemy I., Carreiro C.,
RA Roncal F., Martinez A., Gomez L., Fernandez R., Martinez-A C.,
RA Barbero J.L.;
RT "STAG2 and Rad21 mammalian mitotic cohesins are implicated in meiosis.";
RL EMBO Rep. 3:543-550(2002).
RN [8]
RP POSSIBLE INVOLVEMENT IN POF8.
RX PubMed=22428046; DOI=10.1371/journal.pone.0033412;
RA Caburet S., Zavadakova P., Ben-Neriah Z., Bouhali K., Dipietromaria A.,
RA Charon C., Besse C., Laissue P., Chalifa-Caspi V., Christin-Maitre S.,
RA Vaiman D., Levi G., Veitia R.A., Fellous M.;
RT "Genome-wide linkage in a highly consanguineous pedigree reveals two novel
RT loci on chromosome 7 for non-syndromic familial Premature Ovarian
RT Failure.";
RL PLoS ONE 7:E33412-E33412(2012).
RN [9]
RP INVOLVEMENT IN POF8.
RX PubMed=24597867; DOI=10.1056/nejmoa1309635;
RA Caburet S., Arboleda V.A., Llano E., Overbeek P.A., Barbero J.L., Oka K.,
RA Harrison W., Vaiman D., Ben-Neriah Z., Garcia-Tunon I., Fellous M.,
RA Pendas A.M., Veitia R.A., Vilain E.;
RT "Mutant cohesin in premature ovarian failure.";
RL N. Engl. J. Med. 370:943-949(2014).
CC -!- FUNCTION: Meiosis specific component of cohesin complex. The cohesin
CC complex is required for the cohesion of sister chromatids after DNA
CC replication. The cohesin complex apparently forms a large proteinaceous
CC ring within which sister chromatids can be trapped. At anaphase, the
CC complex is cleaved and dissociates from chromatin, allowing sister
CC chromatids to segregate. The meiosis-specific cohesin complex probably
CC replaces mitosis specific cohesin complex when it dissociates from
CC chromatin during prophase I. {ECO:0000250|UniProtKB:O70576}.
CC -!- SUBUNIT: Component of the meiosis-specific cohesin complex, which also
CC contains the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer. Such complex
CC likely contains RAD21, or the meiosis-specific related protein REC8.
CC Interacts with CCDC79/TERB1; recruiting cohesin to telomeres to develop
CC structural rigidity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00750,
CC ECO:0000269|PubMed:12034751}. Chromosome {ECO:0000269|PubMed:12034751}.
CC Chromosome, centromere {ECO:0000269|PubMed:12034751}. Note=Associates
CC with chromatin. In prophase I stage of meiosis, it is found along the
CC axial elements of synaptonemal complexes. In late-pachytene-diplotene,
CC the bulk of protein dissociates from the chromosome arms probably
CC because of phosphorylation by PLK1, except at centromeres, where
CC cohesin complexes remain. It however remains chromatin associated at
CC the centromeres up to metaphase I. During anaphase I, it probably
CC dissociates from centromeres, allowing chromosomes segregation.
CC {ECO:0000269|PubMed:12034751}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UJ98-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UJ98-2; Sequence=VSP_006996, VSP_006997;
CC Name=3;
CC IsoId=Q9UJ98-3; Sequence=VSP_054742;
CC -!- TISSUE SPECIFICITY: Testis specific.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- DISEASE: Premature ovarian failure 8 (POF8) [MIM:615723]: An ovarian
CC disorder defined as the cessation of ovarian function under the age of
CC 40 years. It is characterized by oligomenorrhea or amenorrhea, in the
CC presence of elevated levels of serum gonadotropins and low estradiol.
CC {ECO:0000269|PubMed:24597867, ECO:0000303|PubMed:22428046}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. A homozygous deletion in STAG3 predicted to result in frameshift
CC and premature truncation, has been shown to be the cause of premature
CC ovarian failure in a large consanguineous family.
CC {ECO:0000269|PubMed:24597867}.
CC -!- SIMILARITY: Belongs to the SCC3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ007798; CAB59367.1; -; mRNA.
DR EMBL; AL833816; CAD38679.2; -; mRNA.
DR EMBL; AK302693; BAG63922.1; -; mRNA.
DR EMBL; AC005071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471091; EAW76568.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76570.1; -; Genomic_DNA.
DR EMBL; BC146806; AAI46807.1; -; mRNA.
DR CCDS; CCDS34703.1; -. [Q9UJ98-1]
DR CCDS; CCDS64730.1; -. [Q9UJ98-3]
DR RefSeq; NP_001269645.1; NM_001282716.1. [Q9UJ98-1]
DR RefSeq; NP_001269646.1; NM_001282717.1.
DR RefSeq; NP_001269647.1; NM_001282718.1. [Q9UJ98-3]
DR RefSeq; NP_036579.2; NM_012447.3. [Q9UJ98-1]
DR AlphaFoldDB; Q9UJ98; -.
DR SMR; Q9UJ98; -.
DR BioGRID; 115957; 12.
DR ComplexPortal; CPX-6082; Nuclear meiotic cohesin complex, STAG3 variant.
DR IntAct; Q9UJ98; 2.
DR STRING; 9606.ENSP00000477973; -.
DR GlyGen; Q9UJ98; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UJ98; -.
DR PhosphoSitePlus; Q9UJ98; -.
DR BioMuta; STAG3; -.
DR DMDM; 68847235; -.
DR EPD; Q9UJ98; -.
DR jPOST; Q9UJ98; -.
DR MassIVE; Q9UJ98; -.
DR MaxQB; Q9UJ98; -.
DR PaxDb; Q9UJ98; -.
DR PeptideAtlas; Q9UJ98; -.
DR PRIDE; Q9UJ98; -.
DR ProteomicsDB; 43653; -.
DR ProteomicsDB; 84605; -. [Q9UJ98-1]
DR ProteomicsDB; 84606; -. [Q9UJ98-2]
DR Antibodypedia; 30623; 168 antibodies from 27 providers.
DR DNASU; 10734; -.
DR Ensembl; ENST00000317296.9; ENSP00000319318.5; ENSG00000066923.18. [Q9UJ98-1]
DR Ensembl; ENST00000394018.6; ENSP00000377586.2; ENSG00000066923.18. [Q9UJ98-3]
DR Ensembl; ENST00000426455.5; ENSP00000400359.1; ENSG00000066923.18. [Q9UJ98-1]
DR Ensembl; ENST00000620100.5; ENSP00000484098.1; ENSG00000066923.18. [Q9UJ98-3]
DR GeneID; 10734; -.
DR KEGG; hsa:10734; -.
DR UCSC; uc003utx.3; human. [Q9UJ98-1]
DR CTD; 10734; -.
DR DisGeNET; 10734; -.
DR GeneCards; STAG3; -.
DR HGNC; HGNC:11356; STAG3.
DR HPA; ENSG00000066923; Tissue enriched (testis).
DR MalaCards; STAG3; -.
DR MIM; 608489; gene.
DR MIM; 615723; phenotype.
DR neXtProt; NX_Q9UJ98; -.
DR OpenTargets; ENSG00000066923; -.
DR Orphanet; 619; NON RARE IN EUROPE: Primary ovarian failure.
DR PharmGKB; PA36178; -.
DR VEuPathDB; HostDB:ENSG00000066923; -.
DR eggNOG; KOG2011; Eukaryota.
DR GeneTree; ENSGT00950000182972; -.
DR InParanoid; Q9UJ98; -.
DR OrthoDB; 167826at2759; -.
DR PhylomeDB; Q9UJ98; -.
DR TreeFam; TF314604; -.
DR PathwayCommons; Q9UJ98; -.
DR Reactome; R-HSA-1221632; Meiotic synapsis.
DR SignaLink; Q9UJ98; -.
DR SIGNOR; Q9UJ98; -.
DR BioGRID-ORCS; 10734; 18 hits in 1082 CRISPR screens.
DR ChiTaRS; STAG3; human.
DR GenomeRNAi; 10734; -.
DR Pharos; Q9UJ98; Tbio.
DR PRO; PR:Q9UJ98; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UJ98; protein.
DR Bgee; ENSG00000066923; Expressed in oocyte and 108 other tissues.
DR ExpressionAtlas; Q9UJ98; baseline and differential.
DR Genevisible; Q9UJ98; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0030893; C:meiotic cohesin complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000795; C:synaptonemal complex; TAS:ProtInc.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0034089; P:establishment of meiotic sister chromatid cohesion; IC:ComplexPortal.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0007130; P:synaptonemal complex assembly; TAS:ProtInc.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039662; Cohesin_Scc3/SA.
DR InterPro; IPR020839; SCD.
DR InterPro; IPR013721; STAG.
DR PANTHER; PTHR11199; PTHR11199; 1.
DR Pfam; PF08514; STAG; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51425; SCD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Centromere; Chromosome;
KW Chromosome partition; Meiosis; Nucleus; Phosphoprotein;
KW Premature ovarian failure; Reference proteome.
FT CHAIN 1..1225
FT /note="Cohesin subunit SA-3"
FT /id="PRO_0000120188"
FT DOMAIN 309..394
FT /note="SCD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00750"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..87
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70576"
FT VAR_SEQ 113..170
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054742"
FT VAR_SEQ 171..212
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_006996"
FT VAR_SEQ 759..1053
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_006997"
FT CONFLICT 309
FT /note="F -> S (in Ref. 3; BAG63922)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="L -> V (in Ref. 1; CAB59367)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="T -> A (in Ref. 1; CAB59367)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="V -> I (in Ref. 1; CAB59367)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="D -> S (in Ref. 1; CAB59367)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="V -> L (in Ref. 1; CAB59367)"
FT /evidence="ECO:0000305"
FT CONFLICT 435..437
FT /note="ASH -> PSN (in Ref. 1; CAB59367)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="C -> Y (in Ref. 3; BAG63922)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="M -> T (in Ref. 1; CAB59367)"
FT /evidence="ECO:0000305"
FT CONFLICT 771
FT /note="S -> W (in Ref. 3; BAG63922)"
FT /evidence="ECO:0000305"
FT CONFLICT 1076
FT /note="R -> K (in Ref. 1; CAB59367)"
FT /evidence="ECO:0000305"
FT CONFLICT 1138
FT /note="G -> GS (in Ref. 2; CAD38679)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1225 AA; 139034 MW; A29B2FC0C3CCE83D CRC64;
MSSPLQRAVG DTKRALSASS SSSASLPFDD RDSNHTSEGN GDSLLADEDT DFEDSLNRNV
KKRAAKRPPK TTPVAKHPKK GSRVVHRHSR KQSEPPANDL FNAVKAAKSD MQSLVDEWLD
SYKQDQDAGF LELVNFFIQS CGCKGIVTPE MFKKMSNSEI IQHLTEQFNE DSGDYPLIAP
GPSWKKFQGS FCEFVRTLVC QCQYSLLYDG FPMDDLISLL TGLSDSQVRA FRHTSTLAAM
KLMTSLVKVA LQLSVHQDNN QRQYEAERNK GPGQRAPERL ESLLEKRKEL QEHQEEIEGM
MNALFRGVFV HRYRDVLPEI RAICIEEIGC WMQSYSTSFL TDSYLKYIGW TLHDKHREVR
LKCVKALKGL YGNRDLTTRL ELFTSRFKDR MVSMVMDREY DVAVEAVRLL ILILKNMEGV
LTDADCESVY PVVYASHRGL ASAAGEFLYW KLFYPECEIR MMGGREQRQS PGAQRTFFQL
LLSFFVESEL HDHAAYLVDS LWDCAGARLK DWEGLTSLLL EKDQNLGDVQ ESTLIEILVS
SARQASEGHP PVGRVTGRKG LTSKERKTQA DDRVKLTEHL IPLLPQLLAK FSADAEKVTP
LLQLLSCFDL HIYCTGRLEK HLELFLQQLQ EVVVKHAEPA VLEAGAHALY LLCNPEFTFF
SRADFARSQL VDLLTDRFQQ ELEELLQSSF LDEDEVYNLA ATLKRLSAFY NTHDLTRWEL
YEPCCQLLQK AVDTGEVPHQ VILPALTLVY FSILWTLTHI SKSDASQKQL SSLRDRMVAF
CELCQSCLSD VDTEIQEQAF VLLSDLLLIF SPQMIVGGRD FLRPLVFFPE ATLQSELASF
LMDHVFIQPG DLGSGDSQED HLQIERLHQR RRLLAGFCKL LLYGVLEMDA ASDVFKHYNK
FYNDYGDIIK ETLTRARQID RSHCSRILLL SLKQLYTELL QEHGPQGLNE LPAFIEMRDL
ARRFALSFGP QQLQNRDLVV MLHKEGIQFS LSELPPAGSS NQPPNLAFLE LLSEFSPRLF
HQDKQLLLSY LEKCLQHVSQ APGHPWGPVT TYCHSLSPVE NTAETSPQVL PSSKRRRVEG
PAKPNREDVS SSQEESLQLN SIPPTPTLTS TAVKSRQPLW GLKEMEEEDG SELDFAQGQP
VAGTERSRFL GPQYFQTPHN PSGPGLGNQL MRLSLMEEDE EEELEIQDES NEERQDTDMQ
ASSYSSTSER GLDLLDSTEL DIEDF
