ID SI1L3_HUMAN Reviewed; 1781 AA.
AC O60292; Q2TV87;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 3.
DT 27-MAR-2024, entry version 175.
DE RecName: Full=Signal-induced proliferation-associated 1-like protein 3;
DE Short=SIPA1-like protein 3;
DE AltName: Full=SPA-1-like protein 3;
GN Name=SIPA1L3; Synonyms=KIAA0545, SPAL3;
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].
RA Matsuura K., Kohu K., Akiyama T.;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 414-1781.
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1544, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1699, AND IDENTIFICATION BY
RP 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1448, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1364, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, AND IDENTIFICATION BY
RP 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 [10]
RP INVOLVEMENT IN CTRCT45.
RX PubMed=25804400; DOI=10.1038/ejhg.2015.46;
RA Evers C., Paramasivam N., Hinderhofer K., Fischer C., Granzow M.,
RA Schmidt-Bacher A., Eils R., Steinbeisser H., Schlesner M., Moog U.;
RT "SIPA1L3 identified by linkage analysis and whole-exome sequencing as a
RT novel gene for autosomal recessive congenital cataract.";
RL Eur. J. Hum. Genet. 23:1627-1633(2015).
RN [11]
RP VARIANT TYR-148, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF
RP VARIANT TYR-148, AND CHROMOSOMAL TRANSLOCATION.
RX PubMed=26231217; DOI=10.1093/hmg/ddv298;
RA Greenlees R., Mihelec M., Yousoof S., Speidel D., Wu S.K., Rinkwitz S.,
RA Prokudin I., Perveen R., Cheng A., Ma A., Nash B., Gillespie R.,
RA Loebel D.A., Clayton-Smith J., Lloyd I.C., Grigg J.R., Tam P.P., Yap A.S.,
RA Becker T.S., Black G.C., Semina E., Jamieson R.V.;
RT "Mutations in SIPA1L3 cause eye defects through disruption of cell polarity
RT and cytoskeleton organization.";
RL Hum. Mol. Genet. 24:5789-5804(2015).
CC -!- FUNCTION: Plays a critical role in epithelial cell morphogenesis,
CC polarity, adhesion and cytoskeletal organization in the lens
CC (PubMed:26231217). {ECO:0000269|PubMed:26231217}.
CC -!- INTERACTION:
CC O60292; P31947: SFN; NbExp=4; IntAct=EBI-2559690, EBI-476295;
CC O60292; P63104: YWHAZ; NbExp=3; IntAct=EBI-2559690, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:26231217}. Note=Detected in tricellular junctions.
CC Colocalizes with apical F-actin. {ECO:0000269|PubMed:26231217}.
CC -!- DISEASE: Note=A chromosomal translocation involving SIPA1L3 is found in
CC a patient with bilateral severe ocular abnormalities including
CC congenital cataracts, corneal clouding, iridocorneal and lenticular
CC adhesions and microphthalmia. Chromosomal translocation
CC t(2;19)(q37.3;q13.1). In addition to translocation, missense variant
CC has been found in patient with bilateral congenital cataracts
CC (PubMed:26231217). {ECO:0000269|PubMed:26231217}.
CC -!- DISEASE: Cataract 45 (CTRCT45) [MIM:616851]: An opacification of the
CC crystalline lens of the eye that frequently results in visual
CC impairment or blindness. Opacities vary in morphology, are often
CC confined to a portion of the lens, and may be static or progressive. In
CC general, the more posteriorly located and dense an opacity, the greater
CC the impact on visual function. {ECO:0000269|PubMed:25804400}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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; AY168880; AAO12531.1; -; mRNA.
DR EMBL; AB011117; BAA25471.2; -; mRNA.
DR EMBL; AC011465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS33007.1; -.
DR RefSeq; NP_055888.1; NM_015073.2.
DR RefSeq; XP_005258728.1; XM_005258671.4.
DR RefSeq; XP_011524959.1; XM_011526657.2.
DR RefSeq; XP_016882006.1; XM_017026517.1.
DR AlphaFoldDB; O60292; -.
DR SMR; O60292; -.
DR BioGRID; 116722; 129.
DR IntAct; O60292; 49.
DR MINT; O60292; -.
DR STRING; 9606.ENSP00000222345; -.
DR iPTMnet; O60292; -.
DR PhosphoSitePlus; O60292; -.
DR BioMuta; SIPA1L3; -.
DR EPD; O60292; -.
DR jPOST; O60292; -.
DR MassIVE; O60292; -.
DR MaxQB; O60292; -.
DR PaxDb; 9606-ENSP00000222345; -.
DR PeptideAtlas; O60292; -.
DR ProteomicsDB; 49323; -.
DR Pumba; O60292; -.
DR Antibodypedia; 59222; 88 antibodies from 21 providers.
DR DNASU; 23094; -.
DR Ensembl; ENST00000222345.11; ENSP00000222345.4; ENSG00000105738.11.
DR GeneID; 23094; -.
DR KEGG; hsa:23094; -.
DR MANE-Select; ENST00000222345.11; ENSP00000222345.4; NM_015073.3; NP_055888.1.
DR UCSC; uc002ohk.4; human.
DR AGR; HGNC:23801; -.
DR CTD; 23094; -.
DR DisGeNET; 23094; -.
DR GeneCards; SIPA1L3; -.
DR HGNC; HGNC:23801; SIPA1L3.
DR HPA; ENSG00000105738; Low tissue specificity.
DR MalaCards; SIPA1L3; -.
DR MIM; 616655; gene.
DR MIM; 616851; phenotype.
DR neXtProt; NX_O60292; -.
DR OpenTargets; ENSG00000105738; -.
DR Orphanet; 98994; Total early-onset cataract.
DR PharmGKB; PA134866783; -.
DR VEuPathDB; HostDB:ENSG00000105738; -.
DR eggNOG; KOG3686; Eukaryota.
DR GeneTree; ENSGT00940000159183; -.
DR HOGENOM; CLU_002127_0_0_1; -.
DR InParanoid; O60292; -.
DR OMA; EDMGEPR; -.
DR OrthoDB; 25782at2759; -.
DR PhylomeDB; O60292; -.
DR TreeFam; TF318626; -.
DR PathwayCommons; O60292; -.
DR SignaLink; O60292; -.
DR BioGRID-ORCS; 23094; 15 hits in 1155 CRISPR screens.
DR ChiTaRS; SIPA1L3; human.
DR GenomeRNAi; 23094; -.
DR Pharos; O60292; Tbio.
DR PRO; PR:O60292; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O60292; Protein.
DR Bgee; ENSG00000105738; Expressed in buccal mucosa cell and 188 other cell types or tissues.
DR ExpressionAtlas; O60292; baseline and differential.
DR Genevisible; O60292; HS.
DR GO; GO:0045177; C:apical part of cell; IMP:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0061689; C:tricellular tight junction; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IDA:UniProtKB.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IDA:UniProtKB.
DR GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 6.10.140.210; -; 1.
DR Gene3D; 3.40.50.11210; Rap/Ran-GAP; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR035974; Rap/Ran-GAP_sf.
DR InterPro; IPR000331; Rap/Ran_GAP_dom.
DR InterPro; IPR021818; SIPA1L_C.
DR PANTHER; PTHR15711; RAP GTPASE-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR15711:SF15; SIGNAL-INDUCED PROLIFERATION-ASSOCIATED 1-LIKE PROTEIN 3; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF21022; Rap-GAP_dimer; 1.
DR Pfam; PF02145; Rap_GAP; 1.
DR Pfam; PF11881; SPAR_C; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF111347; Rap/Ran-GAP; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50085; RAPGAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cataract; Cell membrane; Chromosomal rearrangement;
KW Coiled coil; GTPase activation; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1781
FT /note="Signal-induced proliferation-associated 1-like
FT protein 3"
FT /id="PRO_0000056752"
FT DOMAIN 611..828
FT /note="Rap-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT DOMAIN 966..1042
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 45..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1583..1636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1685..1712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1720..1774
FT /evidence="ECO:0000255"
FT COMPBIAS 45..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1496..1523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:G3X9J0"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:G3X9J0"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1387
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:G3X9J0"
FT MOD_RES 1448
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:G3X9J0"
FT MOD_RES 1619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:G3X9J0"
FT MOD_RES 1622
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:G3X9J0"
FT MOD_RES 1677
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:G3X9J0"
FT MOD_RES 1699
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1703
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:G3X9J0"
FT VARIANT 148
FT /note="D -> Y (found in a patient with bilateral congenital
FT cataracts; uncertain significance; lack of normal basal
FT actin stress fiber formation; absence of SIPA1L3 and F-
FT actin colocalization; dbSNP:rs138476311)"
FT /evidence="ECO:0000269|PubMed:26231217"
FT /id="VAR_075045"
FT VARIANT 1371
FT /note="G -> S (in dbSNP:rs2304133)"
FT /id="VAR_025476"
FT VARIANT 1450
FT /note="P -> A (in dbSNP:rs3745945)"
FT /id="VAR_025477"
SQ SEQUENCE 1781 AA; 194610 MW; 6A91F43B5BC3E175 CRC64;
MTTYRAIPSD GVDLAASCGA RVGDVLPGPH TGDYAPLGFW AQNGSMSQPL GESPATATAT
ATATTRPSPT TPAMPKMGVR ARVADWPPKR EALREHSNPS PSQDTDGTKA TKMAHSMRSI
QNGQPPTSTP ASSGSKAFHR LSRRRSKDVE FQDGWPRSPG RAFLPLRHRS SSEITLSECD
AEDAGEPRGA RHTGALPLFR EYGSTSSIDV QGMPEQSFFD ILNEFRSEQP DARGCQALTE
LLRADPGPHL MGGGGGAKGD SHNGQPAKDS LLPLQPTKEK EKARKKPARG LGGGDTVDSS
IFRKLRSSKP EGEAGRSPGE ADEGRSPPEA SRPWVCQKSF AHFDVQSMLF DLNEAAANRV
SVSQRRNTTT GASAASAASA MASLTASRAH SLGGLDPAFT STEDLNCKEN LEQDLGDDNS
NDLLLSCPHF RNEIGGECER NVSFSRASVG SPSSGEGHLA EPALSAYRTN ASISVLEVPK
EQQRTQSRPR QYSIEHVDLG ARYYQDYFVG KEHANYFGVD EKLGPVAVSI KREKLEDHKE
HGPQYQYRII FRTRELITLR GSILEDATPT ATKHGTGRGL PLKDALEYVI PELNIHCLRL
ALNTPKVTEQ LLKLDEQGLC RKHKVGILYC KAGQSSEEEM YNNEEAGPAF EEFLSLIGEK
VCLKGFTKYA AQLDVKTDST GTHSLYTMYQ DYEIMFHVST LLPYTPNNRQ QLLRKRHIGN
DIVTIIFQEP GALPFTPKNI RSHFQHVFII VRVHNPCTDN VCYSMAVTRS KDAPPFGPPI
PSGTTFRKSD VFRDFLLAKV INAENAAHKS DKFHTMATRT RQEYLKDLAE NCVSNTPIDS
TGKFNLISLT SKKKEKTKAR AGAEQHSAGA IAWRVVAQDY AQGVEIDCIL GISNEFVVLL
DLRTKEVVFN CYCGDVIGWT PDSSTLKIFY GRGDHIFLQA TEGSVEDIRE IVQRLKVMTS
GWETVDMTLR RNGLGQLGFH VKYDGTVAEV EDYGFAWQAG LRQGSRLVEI CKVAVVTLTH
DQMIDLLRTS VTVKVVIIPP FEDGTPRRGW PETYDMNTSE PKTEQESITP GGRPPYRSNA
PWQWSGPASH NSLPASKWAT PTTPGHAQSL SRPLKQTPIV PFRESQPLHS KRPVSFPETP
YTVSPAGADR VPPYRQPSGS FSTPGSATYV RYKPSPERYT AAPHPLLSLD PHFSHDGTSS
GDSSSGGLTS QESTMERQKP EPLWHVPAQA RLSAIAGSSG NKHPSRQDAA GKDSPNRHSK
GEPQYSSHSS SNTLSSNASS SHSDDRWFDP LDPLEPEQDP LSKGGSSDSG IDTTLYTSSP
SCMSLAKAPR PAKPHKPPGS MGLCGGGREA AGRSHHADRR REVSPAPAVA GQSKGYRPKL
YSSGSSTPTG LAGGSRDPPR QPSDMGSRVG YPAQVYKTAS AETPRPSQLA QPSPFQLSAS
VPKSFFSKQP VRNKHPTGWK RTEEPPPRPL PFSDPKKQVD TNTKNVFGQP RLRASLRDLR
SPRKNYKSTI EDDLKKLIIM DNLGPEQERD TGQSPQKGLQ RTLSDESLCS GRREPSFASP
AGLEPGLPSD VLFTSTCAFP SSTLPARRQH QHPHPPVGPG ATPAAGSGFP EKKSTISASE
LSLADGRDRP LRRLDPGLMP LPDTAAGLEW SSLVNAAKAY EVQRAVSLFS LNDPALSPDI
PPAHSPVHSH LSLERGPPTP RTTPTMSEEP PLDLTGKVYQ LEVMLKQLHT DLQKEKQDKV
VLQSEVASLR QNNQRLQEES QAASEQLRKF AEIFCREKKE L
//
