SSH2_HUMAN
ID SSH2_HUMAN Reviewed; 1423 AA.
AC Q76I76; Q8TDB5; Q8WYL1; Q8WYL2; Q96F40; Q96H36; Q9C0D8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Protein phosphatase Slingshot homolog 2;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=SSH-like protein 2;
DE Short=SSH-2L;
DE Short=hSSH-2L;
GN Name=SSH2; Synonyms=KIAA1725, SSH2L;
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] (ISOFORMS 3 AND 4), FUNCTION, INTERACTION WITH
RP ACTIN, AND MUTAGENESIS OF CYS-392.
RX PubMed=11832213; DOI=10.1016/s0092-8674(01)00638-9;
RA Niwa R., Nagata-Ohashi K., Takeichi M., Mizuno K., Uemura T.;
RT "Control of actin reorganization by Slingshot, a family of phosphatases
RT that dephosphorylate ADF/cofilin.";
RL Cell 108:233-246(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=14531860; DOI=10.1046/j.1365-2443.2003.00678.x;
RA Ohta Y., Kousaka K., Nagata-Ohashi K., Ohashi K., Muramoto A., Shima Y.,
RA Niwa R., Uemura T., Mizuno K.;
RT "Differential activities, subcellular distribution and tissue expression
RT patterns of three members of Slingshot family phosphatases that
RT dephosphorylate cofilin.";
RL Genes Cells 8:811-824(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, and Lung;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 282-409 (ISOFORMS 1/4).
RX PubMed=14527359;
RA Chan S.Y., Chan A.K.W., Cheung B.P.K., Liang Y., Leung M.P.;
RT "Identification of genes expressed during myocardial development.";
RL Chin. Med. J. 116:1329-1332(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 382-1423 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND THR-1422, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487 AND THR-1422, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-1217, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 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).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 305-448, AND ACTIVE SITE.
RX PubMed=17427953; DOI=10.1002/prot.21399;
RA Jung S.K., Jeong D.G., Yoon T.S., Kim J.H., Ryu S.E., Kim S.J.;
RT "Crystal structure of human slingshot phosphatase 2.";
RL Proteins 68:408-412(2007).
CC -!- FUNCTION: Protein phosphatase which regulates actin filament dynamics.
CC Dephosphorylates and activates the actin binding/depolymerizing factor
CC cofilin, which subsequently binds to actin filaments and stimulates
CC their disassembly. Inhibitory phosphorylation of cofilin is mediated by
CC LIMK1, which may also be dephosphorylated and inactivated by this
CC protein. {ECO:0000269|PubMed:11832213}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- SUBUNIT: Interacts with filamentous actin.
CC {ECO:0000269|PubMed:11832213}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=L;
CC IsoId=Q76I76-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q76I76-2; Sequence=VSP_016321, VSP_016322, VSP_016323;
CC Name=3; Synonyms=A;
CC IsoId=Q76I76-3; Sequence=VSP_016322, VSP_016323;
CC Name=4;
CC IsoId=Q76I76-4; Sequence=VSP_016324, VSP_016325;
CC -!- MISCELLANEOUS: Tyrosine phosphatase activity has not been demonstrated
CC for this protein to date.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11636.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL92027.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB072358; BAB84117.1; -; mRNA.
DR EMBL; AB072359; BAB84118.1; -; mRNA.
DR EMBL; AB099290; BAC97813.1; -; mRNA.
DR EMBL; BC008941; AAH08941.1; -; mRNA.
DR EMBL; BC011636; AAH11636.2; ALT_INIT; mRNA.
DR EMBL; BC068223; AAH68223.1; -; mRNA.
DR EMBL; AF484838; AAL92027.1; ALT_INIT; mRNA.
DR EMBL; AB051512; BAB21816.1; -; mRNA.
DR CCDS; CCDS11253.1; -. [Q76I76-1]
DR RefSeq; NP_001269058.1; NM_001282129.1.
DR RefSeq; NP_001269059.1; NM_001282130.1.
DR RefSeq; NP_001269060.1; NM_001282131.1.
DR RefSeq; NP_203747.2; NM_033389.3. [Q76I76-1]
DR PDB; 2NT2; X-ray; 2.10 A; A/B/C=305-449.
DR PDBsum; 2NT2; -.
DR AlphaFoldDB; Q76I76; -.
DR SMR; Q76I76; -.
DR BioGRID; 124548; 36.
DR IntAct; Q76I76; 21.
DR MINT; Q76I76; -.
DR STRING; 9606.ENSP00000444743; -.
DR BindingDB; Q76I76; -.
DR ChEMBL; CHEMBL3351198; -.
DR DEPOD; SSH2; -.
DR iPTMnet; Q76I76; -.
DR PhosphoSitePlus; Q76I76; -.
DR BioMuta; SSH2; -.
DR DMDM; 74749833; -.
DR EPD; Q76I76; -.
DR jPOST; Q76I76; -.
DR MassIVE; Q76I76; -.
DR MaxQB; Q76I76; -.
DR PaxDb; Q76I76; -.
DR PeptideAtlas; Q76I76; -.
DR PRIDE; Q76I76; -.
DR ProteomicsDB; 68671; -. [Q76I76-1]
DR ProteomicsDB; 68672; -. [Q76I76-2]
DR ProteomicsDB; 68673; -. [Q76I76-3]
DR ProteomicsDB; 68674; -. [Q76I76-4]
DR Antibodypedia; 26804; 55 antibodies from 20 providers.
DR DNASU; 85464; -.
DR Ensembl; ENST00000269033.7; ENSP00000269033.3; ENSG00000141298.19. [Q76I76-1]
DR GeneID; 85464; -.
DR KEGG; hsa:85464; -.
DR UCSC; uc002heo.3; human. [Q76I76-1]
DR CTD; 85464; -.
DR DisGeNET; 85464; -.
DR GeneCards; SSH2; -.
DR HGNC; HGNC:30580; SSH2.
DR HPA; ENSG00000141298; Tissue enhanced (skeletal).
DR MIM; 606779; gene.
DR neXtProt; NX_Q76I76; -.
DR OpenTargets; ENSG00000141298; -.
DR PharmGKB; PA134861867; -.
DR VEuPathDB; HostDB:ENSG00000141298; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000157430; -.
DR InParanoid; Q76I76; -.
DR PhylomeDB; Q76I76; -.
DR TreeFam; TF319444; -.
DR PathwayCommons; Q76I76; -.
DR SignaLink; Q76I76; -.
DR SIGNOR; Q76I76; -.
DR BioGRID-ORCS; 85464; 23 hits in 1074 CRISPR screens.
DR ChiTaRS; SSH2; human.
DR EvolutionaryTrace; Q76I76; -.
DR GeneWiki; SSH2; -.
DR GenomeRNAi; 85464; -.
DR Pharos; Q76I76; Tbio.
DR PRO; PR:Q76I76; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q76I76; protein.
DR Bgee; ENSG00000141298; Expressed in tibialis anterior and 178 other tissues.
DR ExpressionAtlas; Q76I76; baseline and differential.
DR Genevisible; Q76I76; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:UniProtKB.
DR CDD; cd11652; SSH-N; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR014876; DEK_C.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR043587; Phosphatase_SSH-like.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR043588; SSH-N.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR45864; PTHR45864; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51998; DEK_C; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Hydrolase; Phosphoprotein; Protein phosphatase; Reference proteome.
FT CHAIN 1..1423
FT /note="Protein phosphatase Slingshot homolog 2"
FT /id="PRO_0000094843"
FT DOMAIN 248..303
FT /note="DEK-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT DOMAIN 307..448
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 392
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000269|PubMed:17427953"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SW75"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SW75"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SW75"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SW75"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SW75"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SW75"
FT MOD_RES 1217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1422
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..36
FT /note="MALVTVQRSPTPSTTSSPCASEADSGEEECRSQPRS -> MTLSTLARKRKA
FT PLACTCSLGGPDMIPYFSANAVISQNAINQL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016321"
FT VAR_SEQ 179..195
FT /note="SALQSLHKACEVARAHN -> VDRDSRNKHCYVLLVEE (in isoform 2
FT and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11832213,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016322"
FT VAR_SEQ 196..1423
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11832213,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016323"
FT VAR_SEQ 449
FT /note="S -> R (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11832213"
FT /id="VSP_016324"
FT VAR_SEQ 450..1423
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11832213"
FT /id="VSP_016325"
FT VARIANT 743
FT /note="S -> L (in dbSNP:rs2289629)"
FT /id="VAR_051758"
FT VARIANT 763
FT /note="V -> A (in dbSNP:rs6505140)"
FT /id="VAR_051759"
FT VARIANT 1300
FT /note="H -> Q (in dbSNP:rs8080046)"
FT /id="VAR_051760"
FT MUTAGEN 392
FT /note="C->S: Abrogates phosphatase activity."
FT /evidence="ECO:0000269|PubMed:11832213"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:2NT2"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:2NT2"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:2NT2"
FT HELIX 326..331
FT /evidence="ECO:0007829|PDB:2NT2"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:2NT2"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:2NT2"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:2NT2"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:2NT2"
FT HELIX 371..383
FT /evidence="ECO:0007829|PDB:2NT2"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:2NT2"
FT STRAND 393..397
FT /evidence="ECO:0007829|PDB:2NT2"
FT HELIX 398..411
FT /evidence="ECO:0007829|PDB:2NT2"
FT HELIX 415..425
FT /evidence="ECO:0007829|PDB:2NT2"
FT HELIX 433..447
FT /evidence="ECO:0007829|PDB:2NT2"
SQ SEQUENCE 1423 AA; 158216 MW; 23D0B59C97D6BE38 CRC64;
MALVTVQRSP TPSTTSSPCA SEADSGEEEC RSQPRSISES FLTVKGAALF LPRGNGSSTP
RISHRRNKHA GDLQQHLQAM FILLRPEDNI RLAVRLESTY QNRTRYMVVV STNGRQDTEE
SIVLGMDFSS NDSSTCTMGL VLPLWSDTLI HLDGDGGFSV STDNRVHIFK PVSVQAMWSA
LQSLHKACEV ARAHNYYPGS LFLTWVSYYE SHINSDQSSV NEWNAMQDVQ SHRPDSPALF
TDIPTERERT ERLIKTKLRE IMMQKDLENI TSKEIRTELE MQMVCNLREF KEFIDNEMIV
ILGQMDSPTQ IFEHVFLGSE WNASNLEDLQ NRGVRYILNV TREIDNFFPG VFEYHNIRVY
DEEATDLLAY WNDTYKFISK AKKHGSKCLV HCKMGVSRSA STVIAYAMKE YGWNLDRAYD
YVKERRTVTK PNPSFMRQLE EYQGILLASK QRHNKLWRSH SDSDLSDHHE PICKPGLELN
KKDITTSADQ IAEVKTMESH PPIPPVFVEH MVPQDANQKG LCTKERMICL EFTSREFHAG
QIEDELNLND INGCSSGCCL NESKFPLDNC HASKALIQPG HVPEMANKFP DLTVEDLETD
ALKADMNVHL LPMEELTSPL KDPPMSPDPE SPSPQPSCQT EISDFSTDRI DFFSALEKFV
ELSQETRSRS FSHSRMEELG GGRNESCRLS VVEVAPSKVT ADDQRSSSLS NTPHASEESS
MDEEQSKAIS ELVSPDIFMQ SHSENAISVK EIVTEIESIS QGVGQIQLKG DILPNPCHTP
KKNSIHELLL ERAQTPENKP GHMEQDEDSC TAQPELAKDS GMCNPEGCLT THSSIADLEE
GEPAEGEQEL QGSGMHPGAK WYPGSVRRAT LEFEERLRQE QEHHGAAPTC TSLSTRKNSK
NDSSVADLAP KGKSDEAPPE HSFVLKEPEM SKGKGKYSGS EAGSLSHSEQ NATVPAPRVL
EFDHLPDPQE GPGSDTGTQQ EGVLKDLRTV IPYQESETQA VPLPLPKRVE IIEYTHIVTS
PNHTGPGSEI ATSEKSGEQG LRKVNMEKSV TVLCTLDENL NRTLDPNQVS LHPQVLPLPH
SSSPEHNRPT DHPTSILSSP EDRGSSLSTA LETAAPFVSH TTHLLSASLD YLHPQTMVHL
EGFTEQSSTT DEPSAEQVSW EESQESPLSS GSEVPYKDSQ LSSADLSLIS KLGDNTGELQ
EKMDPLPVAC RLPHSSSSEN IKSLSHSPGV VKERAKEIES RVVFQAGLTK PSQMRRSASL
AKLGYLDLCK DCLPEREPAS CESPHLKLLQ PFLRTDSGMH AMEDQESLEN PGAPHNPEPT
KSFVEQLTTT ECIVQSKPVE RPLVQYAKEF GSSQQYLLPR AGLELTSSEG GLPVLQTQGL
QCACPAPGLA VAPRQQHGRT HPLRRLKKAN DKKRTTNPFY NTM
