DOCK1_MOUSE
ID DOCK1_MOUSE Reviewed; 1865 AA.
AC Q8BUR4; Q3URT8; Q3UY80; Q4QQL8; Q6PD14; Q8BVC9; Q91Z55; Q922V1;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Dedicator of cytokinesis protein 1;
DE AltName: Full=180 kDa protein downstream of CRK;
DE Short=DOCK180;
GN Name=Dock1;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-289 AND 1763-1865 (ISOFORM 1),
RP AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1171-1865 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 902-1865 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, Eye, and Mammary tumor;
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]
RP PHOSPHORYLATION.
RX PubMed=9733740; DOI=10.1074/jbc.273.38.24479;
RA Kiyokawa E., Hashimoto Y., Kurata T., Sugimura H., Matsuda M.;
RT "Evidence that DOCK180 up-regulates signals from the CrkII-p130(Cas)
RT complex.";
RL J. Biol. Chem. 273:24479-24484(1998).
RN [5]
RP INTERACTION WITH ADGRB1 AND ELMO1.
RX PubMed=17960134; DOI=10.1038/nature06329;
RA Park D., Tosello-Trampont A.-C., Elliott M.R., Lu M., Haney L.B., Ma Z.,
RA Klibanov A.L., Mandell J.W., Ravichandran K.S.;
RT "BAI1 is an engulfment receptor for apoptotic cells upstream of the
RT ELMO/Dock180/Rac module.";
RL Nature 450:430-434(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1743; SER-1756; SER-1761;
RP SER-1764; THR-1767; THR-1772 AND SER-1858, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [7]
RP IDENTIFICATION IN A COMPLEX WITH AUTS2 AND ELMO2.
RX PubMed=25533347; DOI=10.1016/j.celrep.2014.11.045;
RA Hori K., Nagai T., Shan W., Sakamoto A., Taya S., Hashimoto R., Hayashi T.,
RA Abe M., Yamazaki M., Nakao K., Nishioka T., Sakimura K., Yamada K.,
RA Kaibuchi K., Hoshino M.;
RT "Cytoskeletal regulation by AUTS2 in neuronal migration and
RT neuritogenesis.";
RL Cell Rep. 9:2166-2179(2014).
CC -!- FUNCTION: Involved in cytoskeletal rearrangements required for
CC phagocytosis of apoptotic cells and cell motility. Along with DOCK1,
CC mediates CRK/CRKL regulation of epithelial and endothelial cell
CC spreading and migration on type IV collagen. Functions as a guanine
CC nucleotide exchange factor (GEF), which activates Rac Rho small GTPases
CC by exchanging bound GDP for free GTP. Its GEF activity may be enhanced
CC by ELMO1. {ECO:0000250|UniProtKB:Q14185}.
CC -!- SUBUNIT: Interacts with the SH3 domains of CRK and NCK2 via multiple
CC sites. Interacts with nucleotide-free RAC1 via its DOCKER domain.
CC Interacts with ELMO1, ELMO2 and probably ELMO3 via its SH3 domain.
CC Interacts with RAC1 (By similarity). Interacts with ELMO1 and ADGRB1
CC (PubMed:17960134). Identified in a complex with AUTS2 and ELMO2
CC (PubMed:25533347). {ECO:0000250|UniProtKB:Q14185,
CC ECO:0000269|PubMed:17960134, ECO:0000269|PubMed:25533347}.
CC -!- INTERACTION:
CC Q8BUR4; Q8BPU7-1: Elmo1; NbExp=13; IntAct=EBI-646023, EBI-644162;
CC Q8BUR4; Q8BYZ7: Elmo3; NbExp=4; IntAct=EBI-646023, EBI-646035;
CC Q8BUR4; Q8C0C0: Zhx2; NbExp=3; IntAct=EBI-646023, EBI-646042;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}.
CC Note=Recruited to membranes via its interaction with
CC phosphatidylinositol 3,4,5-trisphosphate. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BUR4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BUR4-2; Sequence=VSP_022205, VSP_022206;
CC -!- DOMAIN: The DOCKER domain is necessary and sufficient for the GEF
CC activity.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000255|PROSITE-
CC ProRule:PRU00983}.
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DR EMBL; AC100208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC127574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC129300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC136515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC136641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK078899; BAC37448.1; -; mRNA.
DR EMBL; AK082835; BAC38645.1; -; mRNA.
DR EMBL; AK134905; BAE22333.1; -; mRNA.
DR EMBL; AK141224; BAE24599.1; -; mRNA.
DR EMBL; BC006755; AAH06755.1; -; mRNA.
DR EMBL; BC009668; AAH09668.1; -; mRNA.
DR EMBL; BC058998; AAH58998.1; -; mRNA.
DR EMBL; BC098214; AAH98214.1; -; mRNA.
DR CCDS; CCDS40166.1; -. [Q8BUR4-1]
DR RefSeq; NP_001028592.1; NM_001033420.2. [Q8BUR4-1]
DR PDB; 2M0Y; NMR; -; A=1-74.
DR PDBsum; 2M0Y; -.
DR AlphaFoldDB; Q8BUR4; -.
DR BMRB; Q8BUR4; -.
DR SMR; Q8BUR4; -.
DR BioGRID; 237004; 27.
DR IntAct; Q8BUR4; 6.
DR STRING; 10090.ENSMUSP00000081531; -.
DR iPTMnet; Q8BUR4; -.
DR PhosphoSitePlus; Q8BUR4; -.
DR EPD; Q8BUR4; -.
DR jPOST; Q8BUR4; -.
DR MaxQB; Q8BUR4; -.
DR PaxDb; Q8BUR4; -.
DR PeptideAtlas; Q8BUR4; -.
DR PRIDE; Q8BUR4; -.
DR ProteomicsDB; 279796; -. [Q8BUR4-1]
DR ProteomicsDB; 279797; -. [Q8BUR4-2]
DR Antibodypedia; 3822; 289 antibodies from 41 providers.
DR Ensembl; ENSMUST00000084488; ENSMUSP00000081531; ENSMUSG00000058325. [Q8BUR4-1]
DR GeneID; 330662; -.
DR KEGG; mmu:330662; -.
DR UCSC; uc009kdu.1; mouse. [Q8BUR4-2]
DR UCSC; uc009kdv.1; mouse. [Q8BUR4-1]
DR CTD; 1793; -.
DR MGI; MGI:2429765; Dock1.
DR VEuPathDB; HostDB:ENSMUSG00000058325; -.
DR eggNOG; KOG1998; Eukaryota.
DR GeneTree; ENSGT00940000154974; -.
DR HOGENOM; CLU_000595_2_1_1; -.
DR InParanoid; Q8BUR4; -.
DR OMA; RNCVEIR; -.
DR OrthoDB; 102580at2759; -.
DR PhylomeDB; Q8BUR4; -.
DR TreeFam; TF300423; -.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-418885; DCC mediated attractive signaling.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 330662; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Dock1; mouse.
DR PRO; PR:Q8BUR4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BUR4; protein.
DR Bgee; ENSMUSG00000058325; Expressed in dorsal pancreas and 245 other tissues.
DR ExpressionAtlas; Q8BUR4; baseline and differential.
DR Genevisible; Q8BUR4; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IDA:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
DR GO; GO:0007520; P:myoblast fusion; IBA:GO_Central.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 1.20.1270.350; -; 1.
DR Gene3D; 1.20.58.740; -; 1.
DR Gene3D; 1.25.40.410; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027007; C2_DOCK-type_domain.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR026791; DOCK.
DR InterPro; IPR043161; DOCK_C_lobe_A.
DR InterPro; IPR043162; DOCK_C_lobe_C.
DR InterPro; IPR032376; DOCK_N.
DR InterPro; IPR042455; DOCK_N_sub1.
DR InterPro; IPR027357; DOCKER_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR45653; PTHR45653; 1.
DR Pfam; PF06920; DHR-2; 1.
DR Pfam; PF14429; DOCK-C2; 1.
DR Pfam; PF16172; DOCK_N; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51650; C2_DOCK; 1.
DR PROSITE; PS51651; DOCKER; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cytoplasm;
KW Guanine-nucleotide releasing factor; Membrane; Phagocytosis;
KW Phosphoprotein; Reference proteome; SH3 domain; SH3-binding.
FT CHAIN 1..1865
FT /note="Dedicator of cytokinesis protein 1"
FT /id="PRO_0000189985"
FT DOMAIN 9..70
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 425..609
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00983"
FT DOMAIN 1207..1617
FT /note="DOCKER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00984"
FT REGION 1613..1723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1687..1695
FT /note="Phosphoinositide-binding"
FT /evidence="ECO:0000255"
FT REGION 1753..1778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1793..1819
FT /note="Interaction with NCK2 second and third SH3 domain
FT (minor)"
FT /evidence="ECO:0000250"
FT REGION 1801..1865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1820..1836
FT /note="Interaction with NCK2 third SH3 domain (major)"
FT /evidence="ECO:0000250"
FT REGION 1837..1852
FT /note="Interaction with NCK2 (minor)"
FT /evidence="ECO:0000250"
FT MOTIF 1799..1805
FT /note="SH3-binding; interaction with CRK"
FT /evidence="ECO:0000255"
FT MOTIF 1838..1843
FT /note="SH3-binding; interaction with CRK"
FT /evidence="ECO:0000255"
FT COMPBIAS 1633..1662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1676..1715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1823..1853
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1681
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14185"
FT MOD_RES 1743
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1756
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1761
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1764
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1767
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1772
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1858
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1572
FT /note="I -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022205"
FT VAR_SEQ 1573..1865
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022206"
FT CONFLICT 1358
FT /note="I -> V (in Ref. 1; BAE22333)"
FT /evidence="ECO:0000305"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:2M0Y"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:2M0Y"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:2M0Y"
FT STRAND 34..44
FT /evidence="ECO:0007829|PDB:2M0Y"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:2M0Y"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:2M0Y"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:2M0Y"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2M0Y"
SQ SEQUENCE 1865 AA; 215085 MW; 4FFEAA4CBED8DE62 CRC64;
MTRWVPTKRE EKYGVAFYNY DARGADELSL QIGDTVHILE TYEGWYRGYT LRKKSKKGIF
PASYIHLKEA IVEGKGQHET VIPGDLPLIQ EVTTTLREWS TIWRQLYVQD NREMFRSVRH
MIYDLIEWRS QILSGTLPQD ELKELKKKVT AKIDYGNRIL DLDLVVRDED GNILDPELTS
TISLFRAHEV ASKQVEERLQ EEKSQKQNMD INRQAKFAAT PSLALFVNLK NVVCKIGEDA
EVLMSLYDPM ESKFISENYL VRWSSSGLPK DIDRLHNLRA VFTDLGSKDL KREKISFVCQ
IVRVGRMELR DSNTRKLTSG LRRPFGVAVM DVTDIINGKV DDEDKQHFIP FQAVAGENDF
LQTVINKVIA AKEVNHKGQG LWVTLKLLPG DIHQIRKEFP HLVDRTTAVA RKTGFPEIIM
PGDVRNDIYV TLVQGDFDKG SKTTAKNVEV TVSVYDEDGK RLEHVIFPGA GDEAISEYKS
VIYYQVKQPR WFETLKVAIP IEDVNRSHLR FTFRHRSSQD SKDKSEKIFA LAFVKLMRYD
GTTLRDGEHD LIVYKAEAKK LEDAATYLSL PSTKGELEEK GHSATGKGMQ SLGSCTISKD
SFQISTLVCS TKLTQNVDLL GLLKWRSNTN LLQQNLRQLM KVDGGEVVKF LQDTLDALFN
IMMENSESET FDTLVFDALV FIIGLIADRK FQHFNPVLET YIKKHFSATL AYTKLTKVLR
TYVASAEKPG VNEQLYKAIK ALEYIFKFIV RSRVLFNQLY ENKGEADFVE SLLQLFRSIN
DMMSSLSELT VRVKGAALKY LPTIVNDVKL VFDPKELSKM FTEFILNVPA GLLTVQKLSC
LIEIVHSDLF TQHDCREILL PMMTDQLKYH LERQEELEAC CQLLSNILEV LYRKDVGPTQ
RHVQIIMETL LRTVNRTVIS MGRDSELIGN FVACMTAILR QMEDYHYAHL IKTFGKMRTD
VVDFLMETFI MFKNLIGKNV YPFDWVIMNT MQNKVFLRAI NQYADMLNKR FLDQANFELQ
LWNNYFHLAV AFLTQESLQL ENFSSAKRAK ILNKYGDMRR QIGFEIRDMW YNLGQHKIKF
IPEMVGPILE MTLIPETELR KATLPIFFDM MQCEFHSTRS FQMFENEIIT KLDHEVEGGR
GDEQYKVLFD KILLEHCRKH KYLAKTGETF VKLVVRLMER LLDYRTIMHD ENKDNRMSCT
VNVLNFYKEI EREEMYIRYL YKLCDLHKEC DNYTEAAYTL LLHAKLLKWS EDVCAAHLTQ
RDGFQATTQG QLKEQLYQEI IHYFDKGKMW EEAIALGKEL AEQYETEMFD YEQLSELLKK
QAQFYENIVK VIRPKPDYFA VGYYGQGFPS FLRGKVFIYR GKEYERREDF EARLLTQFPN
AEKMKTTSPP GDDIKTSPGQ YIQCFTVKPK LDLPPRFHRP VSEQIVSFYR VNEVQRFEYS
RPIRKGEKNP DNEFANMWIE RTIYTTAYKL PGILRWFEVK SVFMVEISPL ENAIETMQLT
NDKISSMVQQ HLDDPGLPIN PLSMLLNGIV DPAVMGGFAN YEKAFFTDRY LQEHPEAHGQ
IEKLKDLIAW QIPFLAEGIR IHGDKVTEAL RPFHERMEAC FKQLKEKVEK QYGVRTMPSG
LDDRRGSRPR SMVRSFTMPS SSRPLSVASV SSFSSDSTPS RPGSDGFALE PLLPKKMHSR
SQDKLDKDDP DKEKKDKKKE KRNSKHQEIF DKEFKPADSS LQQSEAVILS ETISPLRPQR
PKSQVINVIG NERRFSVSPA SPSSQQTPPP VTPRAKLSFS IQPSLELNGM MGMDVADVPP
PLPLKGNMAD YGNLMENQDM MVSPTSPPPP PPQRQQPPPL PSKTPPPPPP KTTRKQTSVD
SGIVQ
