ID A0A452R8W0_URSAM Unreviewed; 1556 AA.
AC A0A452R8W0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Latent transforming growth factor beta binding protein 4 {ECO:0000313|Ensembl:ENSUAMP00000014904.1};
GN Name=LTBP4 {ECO:0000313|Ensembl:ENSUAMP00000014904.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000014904.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000014904.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSUAMT00000016710.1; ENSUAMP00000014904.1; ENSUAMG00000011598.1.
DR GeneTree; ENSGT00940000158234; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 12.
DR Gene3D; 2.10.25.10; Laminin; 18.
DR Gene3D; 3.90.290.10; TGF-beta binding (TB) domain; 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 PANTHER; PTHR24040:SF13; FIBROPELLIN-1; 1.
DR PANTHER; PTHR24040; LAMININ G-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07645; EGF_CA; 15.
DR Pfam; PF00683; TB; 3.
DR SMART; SM00181; EGF; 18.
DR SMART; SM00179; EGF_CA; 17.
DR SUPFAM; SSF57196; EGF/Laminin; 6.
DR SUPFAM; SSF57184; Growth factor receptor domain; 4.
DR SUPFAM; SSF57581; TB module/8-cys domain; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 11.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS50026; EGF_3; 12.
DR PROSITE; PS01187; EGF_CA; 6.
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:UP000291022};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1556
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018987635"
FT DOMAIN 79..111
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 217..257
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 287..323
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 337..389
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 552..593
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 594..635
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 636..673
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 675..712
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 717..758
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 799..836
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 842..882
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1003..1044
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1135..1189
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1207..1244
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1250..1291
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1303..1356
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT REGION 404..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1407..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1530..1556
FT /note="Disordered"
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 476..490
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 83..93
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 101..110
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 663..672
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1556 AA; 164988 MW; D10390D12B346673 CRC64;
MAGGARVSLM VLLALLGPQP VLGRPRERLR VRFTPAVCGL RCVHGPTGSR CTPTCAPRNA
TSVDSGAPGG AAPGGPGFRA FLCPLICHNG GVCVKPDRCL CPPDFAGKFC QLHSSGARPP
APAMPGLTRS VYTMPLANHR DDEHGVASMV SVHVEHPQEA SVVVHQVERV SGSWEEADAE
AVARAEAAAR AEAAAPYTVL AQSAPREDSY SDASGFGYCF RELRGGECAS PLPGLRTQEV
CCRGAGLAWG VHDCQSCSEH LGISGRVGTP DGPCPTGFER VNGSCQDVDE CATRGRCQHG
ECANTHGGYT CVCPDGFLHD SSRSSCISQH VISEAKGPCF RVLRDGGCSL PILRNITKQI
CCCSRVGKAW GRGCQLCPPF GSEGFREICP AGPGYHYSAS DLRYNTRPLG QEPPRVSLSH
RAPPSTPRPP TGELVSGGGD AISKGLPQPH KEKRRGGTSK FRSPFTDTPS LSGFLPTHRP
EPPPEPRPGP EGQKIQRWGN PGCLASPGPS VGVCQRNPQV CGPGRCIPRP SGYTCACDSG
FRLSPQGTHC VDVDECRRVP PPCAPGRCEN TPGSFHCVCG QGYRAGPRGT ECLDVDECHR
VPPPCDRGRC ENTPGSFLCV CPAGYQAAPH GAGCQDVDEC TQSPGLCGRG VCENLSGSFR
CVCPAGFRGS ACEEDVDECA QEPPPCGPGR CDNTVGSFHC ACPAGFRSRG PGAPCQDVDE
CARSPPPCAY GRCENTEGSF QCVCPTGFQP NTAGSECEDV DECENHLACP GQECVNSPGS
FQCRACPAGH HLHHGRCTDV DECSSGASCG PHGHCTNTEG SFRCSCAPGY RAPSGRPGPC
ADVDECSEED LCQSGICTNT DGSFECVCPP GHRAGPDLAS CLGERRLPGP IPAPLAPLLS
LPCFPHFTAL SSSSDVDECR ERGPALCGSQ RCENSPGSYR CVRDCDPGYH AGPEGTCDDV
DECQEYGSAI CGAQRCENTP GSYRCTPACD PGYQPTPGGG CQDVDECRNQ SFCGAHAVCQ
NLPGSFQCLC DQGYEGARDG RHCVDVNECE TLQGVCGAAL CENVEGSFLC VCPTSPEEFD
PMTGRCVPPR TSAGTFPGSQ PQAPASPGVP ARPPLPSPPR RPSPPRQGPV GSGRRECYFD
TAAPDACDNI LARNVTWQEC CCTVGEGWGS GCRIQQCPST ETAEYQSLCP HGRGYLAPSG
DLSLRRDVDE CQLFRDQVCK SGVCVNTAPG YSCYCSNGYY YHAQRLECVD NDECADEEPA
CEGGSCVNTV GSYHCTCEPP LVLDGSRRRC VSNESQSLDD NLGVCWQEVG ADLVCSRPRL
DRQATYTECC CLYGEAWGMD CALCPAQDSD DFEALCNVLR PPAYGPPRPG GFGLPYEYGP
DLGPPYQGLP YGPELYSPPV LPYDPYPPPP GPFARREAPY GAPPFDMPDF EDDGGPYSES
EAAAPPGPGS RWRYRSRDTR GSFPEPEESP EGGGYPGTLS GPYEGLEAEE CGILDGCAHG
RCVRVPEGFT CDCFSGYRLD MTRMACVGEG RPGPERELSF RRTHPRNSRG LGPQRP
//
