ID F6ZDB7_HORSE Unreviewed; 1841 AA.
AC F6ZDB7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 3.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Latent transforming growth factor beta binding protein 2 {ECO:0000313|Ensembl:ENSECAP00000016809.3};
GN Name=LTBP2 {ECO:0000313|Ensembl:ENSECAP00000016809.3,
GN ECO:0000313|VGNC:VGNC:55288};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000016809.3, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000016809.3, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000016809.3,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000016809.3}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000016809.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR STRING; 9796.ENSECAP00000016809; -.
DR PaxDb; 9796-ENSECAP00000016809; -.
DR Ensembl; ENSECAT00000020479.3; ENSECAP00000016809.3; ENSECAG00000018631.4.
DR VGNC; VGNC:55288; LTBP2.
DR GeneTree; ENSGT00940000160884; -.
DR HOGENOM; CLU_001884_1_0_1; -.
DR InParanoid; F6ZDB7; -.
DR OMA; ADPPHCA; -.
DR Proteomes; UP000002281; Chromosome 24.
DR Bgee; ENSECAG00000018631; Expressed in articular cartilage of joint and 23 other cell types or tissues.
DR ExpressionAtlas; F6ZDB7; baseline.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR GO; GO:0050436; F:microfibril binding; IBA:GO_Central.
DR GO; GO:0097435; P:supramolecular fiber organization; IBA:GO_Central.
DR CDD; cd00054; EGF_CA; 14.
DR Gene3D; 2.10.25.10; Laminin; 19.
DR Gene3D; 3.90.290.10; TGF-beta binding (TB) domain; 4.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
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 PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24034:SF166; VACUOLAR-SORTING RECEPTOR 1; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF07645; EGF_CA; 16.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF00683; TB; 4.
DR SMART; SM00181; EGF; 20.
DR SMART; SM00179; EGF_CA; 18.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57184; Growth factor receptor domain; 5.
DR SUPFAM; SSF57581; TB module/8-cys domain; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 12.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 8.
DR PROSITE; PS50026; EGF_3; 14.
DR PROSITE; PS01187; EGF_CA; 7.
DR PROSITE; PS51364; TB; 4.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..1841
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040254991"
FT DOMAIN 209..241
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 412..444
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 568..609
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 688..740
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 864..906
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 907..943
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 950..989
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1030..1070
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1155..1195
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1196..1237
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1238..1273
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1323..1360
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1431..1483
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1505..1547
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1548..1583
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1604..1656
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1753..1789
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1794..1838
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 37..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 213..223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 231..240
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 416..426
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 434..443
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1552..1562
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1841 AA; 198395 MW; D0A062DFA3893974 CRC64;
MRPPTTVRCP GRARRNPWRS FLPLTLALFV GLGHAQREPV GRQEPAGRDA NRLRRPGGSH
PAAAAAKVYS LFREQDAPLP GLPPTERAQL GWGSPRRPTE AEARRPPRAQ QPRRVQPPAQ
TRRSSPSGQQ QPTPRARAAP VLPRLGTLQR PRAAPPTPPR GRLTGTAGKQ HRGPEAGAQR
SDALLKRRNV CGGQCCPGWT TANSTNFCIK PVCQPPCQNR GSCSRPQLCV CRSGFRGARC
EEVIPEEEFD PQNARPAPRR AAEASPSLRR SSTTREGTVA RTRPPAPQLP LARTLSGLSQ
TQPSQQHVGL SRTVRLYPAP AASGQLTSNA LPAGPGLERR DGAQQAAYLD PLSSPWGLNL
TEKIKKIKIV FTPTICKQTC ARGHCANSCE RGDTTTLYSQ GGHGHDPKSG FRIYFCQIPC
LNGGRCIGRD ECWCPTNSTG KFCHLPAPKL DREPSERGSR HRAPLGGPLR QSTFTLPLSN
QLASVNPSLV KVHIRHPPEA SVQVHQVARV RGEAEEAQEE NSVESRPAPR LPASPSHSHW
DSNSIPARSG EAPRPLPPAA PRPRGLLGRC YLSAVNGQCA NPLLELTAQE DCCGSVGAFW
GVTSCAPCPR RPASPVIENG QLECPKGYKR LNLTHCQDIN ECLTLGLCKD SECVNTRGSY
LCTCRPGLML DPSRSRCVSD KAVSMQQGLC YRSVGPGTCA LPLAQRITKQ ICCCSRVGKA
WGSKCEKCPL LGTEAFKEIC PAGHGYTYSS SDIRLSMRKA EEEELARPSR EQEQKSNRTL
PGPAERQPLR AATDTWLEAE TIPDKGDSQT GQVTTSVTQV PAWVPGDATG RPTPSLPGQG
TPETWQEEQV TTPTDVLVTL APSGIDRCAA GGTNICGPGT CVNLPDGYRC ICNPGYRLHP
SQAYCTDDNE CLRDPCAGKG RCVNRVGSYS CFCYPGYTLV SSGSTQECQD IDECEQPEVC
TGGRCTNTEG SYHCKCDEGY IMVRKGHCQD IDECRHPGTC PDGRCVNSPG SYTCLACEEG
YRGQSGSCID VNECLTPGVC THGKCINLEG SFRCSCEQGY EVTSDEKGCQ DVDECASRAS
CPAGLCLNTE GSFSCSACES GYWVNEDGTA CEDLDECAFP GVCPSGICTN TAGSFSCKDC
EEGYQPSPLG HTCEDVDECE DLQSSCLGGE CKNTAGSYQC LCPQGFQLAN GTVCEDVDEC
MREEYCAPRG ECLNSHGSFF CLCAPGFASA DGGTSCQDVD ECAVTDRCLG GHCVNTEGSF
NCLCDTGFQT SPESGECVDI DECEDSGDSV CGAWRCENSP GSYRCVLGCQ PGFHVAPNGD
CIDIDECAND TVCGSHGFCD NTDGSFRCLC DQGFETSSSG WDCVDVNECE LMLAVCGAAL
CENVEGSFLC LCASDLEEYD AQEGHCRPRV AGGQSIPEAP PGDHLPGPTR MECYSGQNSQ
PHCSSLLGRN TTQAECCCTQ GASWGDACDP CPAEDSVEFS EICPSGKGYI PVEGAWLFGQ
TTYTDADECA MFGPGLCQNG RCLNTVPGYI CLCSPGYHYN AAHRKCEDHD ECQDMACENG
ECVNTEGSFH CFCSPPLTLD LSQQRCVNST SAIEDLPDHD IHMDICWKKV TNYVCSQPLH
GRRTTYTECC CQDGEAWSQQ CALCPPRSSE VYAQLCNVAR IEAEREAGVH FRPGYEYGPG
PEDLHYSLYS PDGAPFYNYL GPEDTIPEPP FPNTASRPGD HTLVLESPLQ PSELQPHYVA
SHPEHQAGFE GLQAEECGIL NGCENGRCVR VREGYTCDCF EGFQLDTAHM ACVDVNECDD
LNGPAALCVH GHCENTEGSY RCHCSPGYVA EAGPPHCIAK E
//
