PDS5B_MOUSE
ID PDS5B_MOUSE Reviewed; 1446 AA.
AC Q4VA53; Q3TNZ4; Q7TSS4; Q80TM8; Q8BJ18; Q8BLH6; Q8BX77;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Sister chromatid cohesion protein PDS5 homolog B;
DE AltName: Full=Androgen-induced proliferation inhibitor;
DE AltName: Full=Androgen-induced prostate proliferative shutoff-associated protein AS3;
GN Name=Pds5b;
GN Synonyms=Aprin, As3 {ECO:0000303|Ref.1},
GN Kiaa0979 {ECO:0000312|EMBL:BAC65696.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAM52216.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAM52216.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAM52216.1};
RA Geck P., Maffini M., Sonnenschein C., Soto A.M.;
RT "The AS3 proliferative arrest gene has an ancient eukaryotic heritage and
RT shows highly conserved functional domains in mice.";
RL Proc. Annu. Meet. Am. Assoc. Cancer Res. 43:987-987(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC32242.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 625-1446 (ISOFORM 3), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 1092-1446 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC32242.1};
RC TISSUE=Cerebellum {ECO:0000312|EMBL:BAC33427.1},
RC Embryo {ECO:0000312|EMBL:BAC32242.1}, Head {ECO:0000312|EMBL:BAE37943.1},
RC and Thymus {ECO:0000312|EMBL:BAC31031.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH96539.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH96539.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH96539.1};
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 [4] {ECO:0000305, ECO:0000312|EMBL:BAC65696.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 256-1446 (ISOFORM 1).
RC TISSUE=Brain {ECO:0000312|EMBL:BAC65696.1};
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1356, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1356, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1166; THR-1253; SER-1257;
RP SER-1281 AND SER-1356, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1162; SER-1166; SER-1176;
RP SER-1182; SER-1255; SER-1257; SER-1281; SER-1356; SER-1364; SER-1367;
RP THR-1368; SER-1415 AND SER-1418, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1136, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Regulator of sister chromatid cohesion in mitosis which may
CC stabilize cohesin complex association with chromatin. May couple sister
CC chromatid cohesion during mitosis to DNA replication. Cohesion ensures
CC that chromosome partitioning is accurate in both meiotic and mitotic
CC cells and plays an important role in DNA repair. Plays a role in
CC androgen-induced proliferative arrest in prostate cells (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the cohesin complex. Interacts with RAD21; the
CC interaction is direct. Interacts with WAPL (via FGF motifs) or CDCA5
CC (via the FGF motif); the interaction is direct, cohesin-dependent and
CC competitive (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6TRW4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|Ref.1};
CC IsoId=Q4VA53-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=Q4VA53-2; Sequence=VSP_052403, VSP_052405, VSP_052406;
CC Name=3 {ECO:0000269|PubMed:16141072};
CC IsoId=Q4VA53-3; Sequence=VSP_052404;
CC -!- TISSUE SPECIFICITY: Expressed in prostate. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the PDS5 family. {ECO:0000305}.
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DR EMBL; AY102267; AAM52216.1; -; mRNA.
DR EMBL; AK041682; BAC31031.1; -; mRNA.
DR EMBL; AK045159; BAC32242.1; -; mRNA.
DR EMBL; AK048706; BAC33427.1; -; mRNA.
DR EMBL; AK164853; BAE37943.1; -; mRNA.
DR EMBL; BC096539; AAH96539.1; -; mRNA.
DR EMBL; AK122414; BAC65696.1; -; mRNA.
DR CCDS; CCDS39412.1; -. [Q4VA53-1]
DR CCDS; CCDS85012.1; -. [Q4VA53-3]
DR RefSeq; NP_001333432.1; NM_001346503.1. [Q4VA53-3]
DR RefSeq; NP_780519.3; NM_175310.6. [Q4VA53-1]
DR AlphaFoldDB; Q4VA53; -.
DR SMR; Q4VA53; -.
DR BioGRID; 221515; 6.
DR IntAct; Q4VA53; 1.
DR MINT; Q4VA53; -.
DR STRING; 10090.ENSMUSP00000016569; -.
DR GlyConnect; 2716; 3 N-Linked glycans (1 site).
DR GlyGen; Q4VA53; 1 site, 3 N-linked glycans (1 site).
DR iPTMnet; Q4VA53; -.
DR PhosphoSitePlus; Q4VA53; -.
DR EPD; Q4VA53; -.
DR jPOST; Q4VA53; -.
DR MaxQB; Q4VA53; -.
DR PaxDb; Q4VA53; -.
DR PeptideAtlas; Q4VA53; -.
DR PRIDE; Q4VA53; -.
DR ProteomicsDB; 288092; -. [Q4VA53-1]
DR ProteomicsDB; 288093; -. [Q4VA53-2]
DR ProteomicsDB; 288094; -. [Q4VA53-3]
DR Antibodypedia; 22916; 179 antibodies from 29 providers.
DR DNASU; 100710; -.
DR Ensembl; ENSMUST00000016569; ENSMUSP00000016569; ENSMUSG00000034021. [Q4VA53-1]
DR Ensembl; ENSMUST00000110486; ENSMUSP00000106112; ENSMUSG00000034021. [Q4VA53-2]
DR Ensembl; ENSMUST00000202170; ENSMUSP00000144572; ENSMUSG00000034021. [Q4VA53-3]
DR GeneID; 100710; -.
DR KEGG; mmu:100710; -.
DR UCSC; uc009auh.2; mouse. [Q4VA53-1]
DR UCSC; uc009aui.1; mouse. [Q4VA53-2]
DR UCSC; uc009auj.2; mouse. [Q4VA53-3]
DR CTD; 23047; -.
DR MGI; MGI:2140945; Pds5b.
DR VEuPathDB; HostDB:ENSMUSG00000034021; -.
DR eggNOG; KOG1525; Eukaryota.
DR GeneTree; ENSGT00940000157257; -.
DR HOGENOM; CLU_004041_0_0_1; -.
DR InParanoid; Q4VA53; -.
DR OMA; CFDIVSG; -.
DR PhylomeDB; Q4VA53; -.
DR TreeFam; TF106415; -.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2468052; Establishment of Sister Chromatid Cohesion.
DR Reactome; R-MMU-2470946; Cohesin Loading onto Chromatin.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR BioGRID-ORCS; 100710; 9 hits in 71 CRISPR screens.
DR ChiTaRS; Pds5b; mouse.
DR PRO; PR:Q4VA53; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q4VA53; protein.
DR Bgee; ENSMUSG00000034021; Expressed in renal medulla interstitium and 246 other tissues.
DR ExpressionAtlas; Q4VA53; baseline and differential.
DR Genevisible; Q4VA53; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0097402; P:neuroblast migration; IMP:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039776; Pds5.
DR PANTHER; PTHR12663; PTHR12663; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1446
FT /note="Sister chromatid cohesion protein PDS5 homolog B"
FT /id="PRO_0000287425"
FT REPEAT 383..419
FT /note="HEAT"
FT /evidence="ECO:0000255"
FT DNA_BIND 1247..1259
FT /note="A.T hook 1"
FT /evidence="ECO:0000255"
FT DNA_BIND 1285..1297
FT /note="A.T hook 2"
FT /evidence="ECO:0000255"
FT DNA_BIND 1370..1382
FT /note="A.T hook 3"
FT /evidence="ECO:0000255"
FT REGION 1137..1446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1136
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NTI5"
FT MOD_RES 1162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NTI5"
FT MOD_RES 1253
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 1255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:16452087, ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1365
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NTI5"
FT MOD_RES 1367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1368
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NTI5"
FT MOD_RES 1415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..529
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052403"
FT VAR_SEQ 1206
FT /note="L -> LVR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052404"
FT VAR_SEQ 1207..1230
FT /note="SELEKPRSRKKAPVTDPEEKLGMD -> VRVRCLVGRVMRLLIVIVLVIFAL
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052405"
FT VAR_SEQ 1231..1446
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052406"
FT CONFLICT 496
FT /note="W -> R (in Ref. 1; AAM52216)"
FT /evidence="ECO:0000305"
FT CONFLICT 966
FT /note="I -> T (in Ref. 1; AAM52216)"
FT /evidence="ECO:0000305"
FT CONFLICT 978
FT /note="A -> S (in Ref. 1; AAM52216)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1446 AA; 164419 MW; 3540041DE3C7FCBE CRC64;
MAHSKTRTND GKITYPPGVK EISDKISKEE MVRRLKMVVK TFMDMDQDSE EEKELYLNLA
LHLASDFFLK HPDKDVRLLV ACCLADIFRI YAPEAPYTSP DKLKDIFMFI TRQLKGLEDT
KSPQFNRYFY LLENIAWVKS YNICFELEDS NEIFTQLYRT LFSVINNGHN QKVHMHMVDL
MSSIICEGDT VSQELLDTVL VNLVPAHKNL NKQAYDLAKA LLKRTAQAIE PYITNFFNQV
LMLGKTSISD LSEHVFDLIL ELYNIDSHLL LSVLPQLEFK LKSNDNEERL QVVKLLAKMF
GAKDSELASQ NKPLWQCYLG RFNDIHVPIR LECVKFASHC LMNHPDLAKD LTEYLKVRSH
DPEEAIRHDV IVSIVTAAKK DILLVNDHLL NFVRERTLDK RWRVRKEAMM GLAQIYKKYS
LQSAAGKDAA KQISWVKDKL LHIYYQNSID DRLLVERIFA QYMVPHNLET TERMKCLYYL
YATLDLNAVK ALNEMWKCQN LLRHQVKDLL DLIKQPKTDA SVKAIFSKVM VITRNLPDPG
KAQDFMKKFT QVLEDDEKIR KQLEALVSPT CSCKQAEGCV REITKKLGNP KQPTNPFLEM
IKFLLERIAP VHIDTESISA LIKQVNKSID GTADDEDEGV PTDQAIRAGL ELLKVLSFTH
PISFHSAETF ESLLACLKMD DEKVAEAALQ IFKNTGSKIE EDFPHIRSAL LPVLHHKSKK
GPPRQAKYAI HCIHAIFSSK ETQFAQIFEP LHKSLDPSNL EHLITPLVTI GHIALLAPDQ
FAAPLKSLVA TFIVKDLLMN DRLPGKKTTK LWVPDEEVSP ETMVKIQAIK MMVRWLLGMK
NNHSKSGTST LRLLTTILHS DGDLTEQGKI SKPDMSRLRL AAGSAIVKLA QEPCYHEIIT
LEQYQLCALA INDECYQVRQ VFAQKLHKGL SRLRLPLEYM AICALCAKDP VKERRAHARQ
CLVKNITVRR EYLKQHAAVS EKLLSLLPEY VVPYTIHLLA HDPDYVKVQD IEQLKDVKEC
LWFVLEILMA KNENNSHAFI RKMVENIKQT KDAQGPDDTK MNEKLYTVCD VAMNIIMSKS
TTYSLESPKD PVLPARFFTQ PDKNFSNTKN YLPPEMKSFF TPGKPKTANV LGAVNKPLSS
AGKQSQTKSS RMETVSNASS SSNPSSPGRI KGRLDSSEMD HSENEDYTMS SPLPGKKSDK
REDPDLSELE KPRSRKKAPV TDPEEKLGMD DLTKLVQEQK PKGSQRGRKR GRTASDSDEQ
QWPEEKRHKE ELLENEDEQN SPPKKGKRGR PPKPLGGGTS KEEPTMKTSK KGNKKKLVPP
VVDDDEEEER QIGNTEHKSK SKQHRTSKRA QQRAESPETS AVESTQSTPQ KGRGRPSKAP
SPSQPPKKIR VGRSKQVATK ENDSSEEMDV LQASSPVSDD TTQEGAEEED ISVGNVRRRS
SKRERR
