LTBP2_BOVIN
ID LTBP2_BOVIN Reviewed; 1842 AA.
AC Q28019;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Latent-transforming growth factor beta-binding protein 2;
DE Short=LTBP-2;
DE Flags: Precursor;
GN Name=LTBP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8524260; DOI=10.1128/mcb.15.12.6932;
RA Gibson M.A., Hatzinikolas G., Davis E.C., Baker E., Sutherland G.R.,
RA Mecham R.P.;
RT "Bovine latent transforming growth factor beta 1-binding protein 2:
RT molecular cloning, identification of tissue isoforms, and
RT immunolocalization to elastin-associated microfibrils.";
RL Mol. Cell. Biol. 15:6932-6942(1995).
RN [2]
RP REVIEW.
RX PubMed=10743502; DOI=10.1016/s1359-6101(99)00010-6;
RA Saharinen J., Hyytiainen M., Taipale J., Keski-Oja J.;
RT "Latent transforming growth factor-beta binding proteins (LTBPs)
RT -- structural extracellular matrix proteins for targeting TGF-beta
RT action.";
RL Cytokine Growth Factor Rev. 10:99-117(1999).
RN [3]
RP REVIEW.
RX PubMed=11104663; DOI=10.1042/bj3520601;
RA Oklu R., Hesketh R.;
RT "The latent transforming growth factor beta binding protein (LTBP)
RT family.";
RL Biochem. J. 352:601-610(2000).
CC -!- FUNCTION: May play an integral structural role in elastic-fiber
CC architectural organization and/or assembly.
CC {ECO:0000250|UniProtKB:Q14767}.
CC -!- SUBUNIT: Forms part of the large latent transforming growth factor beta
CC precursor complex; removal is essential for activation of complex.
CC Interacts with SDC4. Interacts (via C-terminal domain) with FBN1 (via
CC N-terminal domain) in a Ca(+2)-dependent manner.
CC {ECO:0000250|UniProtKB:Q14767}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:8524260}.
CC -!- TISSUE SPECIFICITY: Localized in nuchal ligament and aorta to the
CC fibrillin-containing, microfibrillar component of elastic fibers (at
CC protein level). {ECO:0000269|PubMed:8524260}.
CC -!- PTM: N-Glycosylated. {ECO:0000250|UniProtKB:Q14767}.
CC -!- PTM: Contains hydroxylated asparagine residues.
CC {ECO:0000250|UniProtKB:Q14766}.
CC -!- SIMILARITY: Belongs to the LTBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA91455.1; Type=Erroneous initiation; Evidence={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; U35363; AAA91455.1; ALT_INIT; mRNA.
DR RefSeq; NP_776810.1; NM_174385.2.
DR AlphaFoldDB; Q28019; -.
DR STRING; 9913.ENSBTAP00000029274; -.
DR PaxDb; Q28019; -.
DR PRIDE; Q28019; -.
DR GeneID; 281905; -.
DR KEGG; bta:281905; -.
DR CTD; 4053; -.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; Q28019; -.
DR OrthoDB; 1174178at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0071953; C:elastic fiber; IDA:AgBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0001527; C:microfibril; IDA:AgBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0050436; F:microfibril binding; IDA:AgBase.
DR GO; GO:0097435; P:supramolecular fiber organization; IBA:GO_Central.
DR Gene3D; 3.90.290.10; -; 4.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR017878; TB_dom.
DR InterPro; IPR036773; TB_dom_sf.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF07645; EGF_CA; 16.
DR Pfam; PF00683; TB; 4.
DR SMART; SM00181; EGF; 20.
DR SMART; SM00179; EGF_CA; 18.
DR SUPFAM; SSF57184; SSF57184; 5.
DR SUPFAM; SSF57581; SSF57581; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 13.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 11.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS01187; EGF_CA; 16.
DR PROSITE; PS51364; TB; 4.
PE 1: Evidence at protein level;
KW Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW Growth factor binding; Heparin-binding; Hydroxylation; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000250|UniProtKB:O35806"
FT CHAIN 36..1842
FT /note="Latent-transforming growth factor beta-binding
FT protein 2"
FT /id="PRO_0000007642"
FT DOMAIN 181..213
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 384..416
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 540..592
FT /note="TB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 610..650
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 660..712
FT /note="TB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 836..878
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 879..921
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 922..961
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 962..1001
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1002..1042
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1043..1084
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1085..1126
FT /note="EGF-like 10; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1127..1167
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1168..1209
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1210..1250
FT /note="EGF-like 13; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1251..1294
FT /note="EGF-like 14; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1295..1336
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1337..1379
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1403..1455
FT /note="TB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 1477..1519
FT /note="EGF-like 17; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1520..1559
FT /note="EGF-like 18; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1576..1628
FT /note="TB 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 1754..1794
FT /note="EGF-like 19; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1795..1839
FT /note="EGF-like 20; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 38..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..114
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 219..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..243
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 295..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1631..1842
FT /note="C-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:Q14767"
FT MOTIF 363..365
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 113..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 332..342
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08999"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 185..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 189..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 203..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 388..398
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 392..404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 406..415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 542..564
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 551..577
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 565..580
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 614..625
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 620..634
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 636..649
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 662..684
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 671..697
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 685..700
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 686..712
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 840..853
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 848..862
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 864..877
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 883..894
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 888..903
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 905..920
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 926..937
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 932..946
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 948..960
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 966..977
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 972..986
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 989..1000
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1006..1017
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1012..1026
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1028..1041
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1047..1058
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1053..1067
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1070..1083
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1089..1100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1095..1109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1112..1125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1131..1143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1138..1152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1154..1166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1172..1184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1178..1193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1195..1208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1214..1225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1220..1234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1236..1249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1255..1268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1263..1277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1281..1293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1299..1311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1305..1320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1322..1335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1341..1353
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1348..1362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1364..1378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1405..1428
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1415..1440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1429..1443
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1430..1455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1481..1494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1489..1503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1505..1518
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1524..1534
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1529..1543
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1545..1558
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1578..1601
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1587..1613
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1602..1616
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1603..1628
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1758..1769
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1764..1778
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1780..1793
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1799..1814
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1809..1823
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1825..1838
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1842 AA; 198410 MW; 5C06161EA29AB6AA CRC64;
MRPPTTARCP GRVLQNPWRS FWPLTLALFV GMGQAQRDPV GRYEPAGRDA SRLRRPGGSP
VVATAKVYSL FREQDAPVRG SPPAELVQPS WGSPRRSTEA EARRPPRAQQ PRRVQPPAQT
WRSRPSGQQQ SAPRARAAPA LPRLETVQRP RAARGRLTGR NVCGGQCCPG WTTANSTNHC
IKPVCQPPCQ NRGSCSRPQL CVCRSGFRGA RCEEVIPEEE FDPQNSRPAP RRSAEGPPSL
RRSSVAREST TARVRPPAPQ LQRARTLSGL SQTRSSQQHV GLSQTTRLYP APAASGQLTS
NALPMGPGPE RRDGAPQAAY LDRPSSSWGL NLTEKIKKIK IVFTPTICKQ TCARGRCANS
CERGDTTTLY SQSGHGHDPK SGFRIYFCQI PCLNGGRCIG RDECWCPANS TGKFCHLPAP
RLDQEPPERG PRHRAPLEGP LKQSTFTLPL SNQLASVNPS LVNVHIRHPP EASVQIHQVA
RVRGEAEEAP EENSVETRPS PRLPAGPGPG RWDSNRIPAR SGEAPRLPPP VVPRTPALLG
RCYLSTLNGQ CANPLPELTA HEDCCGSVGA FWGVTSCAPC PPRPASPVIE NGQLECPQGY
KRLNLTHCED VNECLTLGLC EDSECVNTRG SYLCTCRPGL LLDPSRSRCV SDKAVSMQQG
LCYRLLGPGT CALPLAQRIT KQICCCSRVG KAWGSLCEKC PLPGTEAFRE ICPAGHGYTY
SSSDIRLSMR KAEEEELARP SRDRGPKRNG TLPRPAERQP LRAATGTWVE AETIPDKGDS
QASQVTTSVT QLSTWVPGGA LGTPTPSVPE QGIPEAREEA QVTAPTNVLV TPAPSGIDRC
AAGATNICGP GTCVNLPDGY RCICSPGYRL HPSQAYCTDD NECLRDPCKG RGRCVNRVGS
YSCFCYPGYK LATSGATQEC QDIDECEQPG VCSRGRCTNT EGSYHCECDQ GYIMVRKGHC
QDINECRHPG TCPDGKCVNS PGSYTCLPCE EGYRGQGGSC VDVNECLTPG VCTHGTCINL
EGSFRCSCEQ GYEVTPDEKG CKDVDECAIR ASCPTGLCLN TEGSFTCSAC ESGYWVNEDG
TACEDLDECA FPGVCPSGVC TNTAGSFSCR DCEAGYQPSA LGHTCEDVDE CEDPQSSCLG
GECKNTAGSY QCLCPPGFQL ANGTVCEDVD ECVGEEYCAP RGECLNSHGS FFCLCADGFV
SADGGTSCQD VDECAVTDRC VGGQCVNTDG SFNCVCETGF QPSPESGECV DIDECEDLGE
PICGAWRCEN SPGSYRCVLG CQPGFHMAPT GDCIDIDECA NDTVCGSHGF CDNTDGAFRC
LCDQGFETSP SGWDCVDVNE CELMLAVCGA ALCENVEGSF LCLCASDLEE YDAQEGRCRP
RGAGGPSVPE ARPGAHPPGP VRMECYSGQK DQTPCSSLLG RNTTQAECCC TQGTGWGDAC
DLCPDEDSVE FSEICPSGKG YIPVEGAWMF GQTTYTDADE CVMFGPGLCR NGRCLNTVPG
YICLCNPGYH YNAASRKCED HDECQDMACE NGECVNTEGS FHCFCSPPLT LDLSQQRCVN
STSGVEDLPD HDIHMDICWK RVTNYVCSHP LHGRRTTYTE CCCQDGEAWS QQCALCPPRS
SEVYAQLCNV ARIEAEREAG IHFRPGYEYS PGPDDLHYSL YGPDGVPFYN YLGPEDAIPE
PLFPSTAGRP GDRIPLPEPP LQPSELQPHY VASHPGLCCC KNGEEVGSEA VSLPSSPSAH
HCQQEHQAGF EGLQAEECGI LNGCENGRCV RVREGYTCDC FEGFQLDTAH MACVDVNECD
DLNGPAALCV HGHCDNTEGS YRCHCLPGYV AEAGPPHCTA KE
