ID A0A3B4TUV0_SERDU Unreviewed; 1371 AA.
AC A0A3B4TUV0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Latent transforming growth factor beta binding protein 4 {ECO:0008006|Google:ProtNLM};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000009802.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000009802.1}
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 STRING; 41447.ENSSDUP00000009802; -.
DR Ensembl; ENSSDUT00000009991.1; ENSSDUP00000009802.1; ENSSDUG00000007151.1.
DR GeneTree; ENSGT00940000158234; -.
DR OMA; NHAGICE; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 9.
DR Gene3D; 2.10.25.10; Laminin; 13.
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; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24034:SF111; FIBRILLIN-3; 1.
DR Pfam; PF07645; EGF_CA; 12.
DR Pfam; PF00683; TB; 4.
DR SMART; SM00181; EGF; 14.
DR SMART; SM00179; EGF_CA; 14.
DR SUPFAM; SSF57196; EGF/Laminin; 7.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR SUPFAM; SSF57581; TB module/8-cys domain; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 8.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 5.
DR PROSITE; PS50026; EGF_3; 9.
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..1371
FT /note="Latent transforming growth factor beta binding
FT protein 4"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017226711"
FT DOMAIN 132..164
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 230..271
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 295..331
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 345..401
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 517..558
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 559..596
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 637..678
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 679..719
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 966..1019
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1034..1076
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1077..1112
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1125..1174
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1325..1369
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1174..1255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1219
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 136..146
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 154..163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 563..573
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1081..1091
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1371 AA; 147777 MW; 549023F97B63549D CRC64;
MICWITSSIL ALVSCCEEVR ISQQTVCLPA PSPLSRGGRR GGCWKGQEAI SASREEATSI
LTASGGLHPG HEVTAPNLAS SKATFPAQQA VVSGSHVTVP SSTLSSCEKP RGPWGADPML
RWRIQCFSVC AQRFLCPLLC KNGGVCLQKD RCFCPPNFTG KFCQIPVAPT SAAASPAAAA
PSSTNEIVKP APSMVKVRVQ HPPEASVKIH QVVKVRTLSC FSCARTLTGN VCVCVCVRVQ
CSSPLPGLRS REMCCRGIGK GWGITDCVLC PDSTVESNSS CPVGFEQANG TQCVDVNECL
QPGLCENGIC VNTRGSYSCV CRAGFILDAS HGICISQSVI SEEKGQCHRV LGSGQGPSSC
SLPILRNITK QICCCSRVGK AWGPDCQRCP YFGSVAFKEI CPAGPGYHYS ASALQFNQRV
TQQLGGRGAP LVPHGSQENQ GSYSRPSSFV QHSPSKLSQC HTEINNCTYW CVFMSVNNSE
CLYLCVCVCV CVCVSVCVCV CVCVCVCMCM CVCVSVDVNE CVQSPGVCSV GECVNTMGSY
RCVCPSGYRS SSQQTSCQDI DECQLNPCRN GRCENMPGSY RCVCRLGYRL TGNTCTDVDE
CEDPLQCPGQ ECINSPGSYR CASCQPGYGL LNRLCTDIDE CASTGACEPE RVCVNTVGSF
RCDCPPGYRT SGLGRQCRDI NECLESDFCF SGGECVNTPG SYSCCQTGFT TNPEKTTCLG
THTHTHKKLC LTSISCAEPK DCSCCHLIND CLKYHLAFRR PPVTKDVFRI MALLCGHLRA
TVLPHKSCVF YNVDVQHISL SDVDECVSSG GSVCGSQRCE NTIGSYRCLT SCEPGYQVTQ
SGKCVDINEC TNKTVCGDHA FCQNLIGTYL CVCDMACVGM YEDECVSLQD ACGSARCENM
EGSFICVCDE LEEFDVAAGK CVSPVQSGTL NFFFLLLQQW APTTLPPPLP PPRPHPLHPH
PSMSLRECYY NLAEQGTCSL LATNTSQQEC CCTLGEAWGL GCQYHACPPT DTAGFLSLCP
SGRGYVTTGP GAFNVDECKR FHLEVCKNGV CVNNIPGYSC YCSSGYVYNS TLLECVDHDE
CEEESCVGGV CVNTVGSYYC SCQPPLVLDD TQRNCVNSSH LTNLSVCWQH VSADLMCQSP
LLGAQVTFTI CCCLYGEGWG MECALCPSTN SGDYGSPDGS QPRPPSFQLP PDPRAETAFG
ARPPPPSRPD GPPLSLAPLP GAPYEDQEVE EEEEETWRPG PPFTPFTERS RGGVAGPRRV
YESESTWWCS AAFYPTRSFA GLSAAEDCGI LHGCENGRCI RVAEGYTCDC YQGYELDMAS
MTCIDVNECE DSVSVEFPCV NARCVNTEGS FRCVCRRGYI MSRRPNHCVA A
//
