ID A0A3B3RR58_9TELE Unreviewed; 1180 AA.
AC A0A3B3RR58;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Latent-transforming growth factor beta-binding protein 3-like {ECO:0000313|Ensembl:ENSPKIP00000021062.1};
GN Name=LTBP3 {ECO:0000313|Ensembl:ENSPKIP00000021062.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000021062.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000021062.1}
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 AlphaFoldDB; A0A3B3RR58; -.
DR Ensembl; ENSPKIT00000001688.1; ENSPKIP00000021062.1; ENSPKIG00000005539.1.
DR GeneTree; ENSGT00940000160285; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 12.
DR Gene3D; 2.10.25.10; Laminin; 16.
DR Gene3D; 3.90.290.10; TGF-beta binding (TB) domain; 4.
DR InterPro; IPR026823; cEGF.
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; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 12.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF00683; TB; 4.
DR SMART; SM00181; EGF; 16.
DR SMART; SM00179; EGF_CA; 15.
DR SUPFAM; SSF57196; EGF/Laminin; 6.
DR SUPFAM; SSF57184; Growth factor receptor domain; 4.
DR SUPFAM; SSF57581; TB module/8-cys domain; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 13.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 8.
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1..24
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 128..171
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 206..244
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 251..303
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 407..448
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 449..486
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 493..535
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 576..616
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 617..657
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 658..697
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 698..740
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 750..804
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 868..904
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 961..997
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1011..1064
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1132..1173
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 339..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 14..23
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1180 AA; 130607 MW; FE72413CC799D408 CRC64;
MNGGVCSSHS HCLCPPGFTG RLCQFSIRKT QEAQAAVGNK QPAYSLQLVP EVSGPGEQGR
GHMAQTHSVF SLPLAPGVGH HSQEVQFNVR VHHTSDTAVV IHPVDHSDGK PPHKTTVRLM
PQTHKPRGRC FQETTPKQAC SSNPLPGLTN QEDCCGSVGN SWGQNKCYKC PKLLYPGVHK
PHTIIEEYGP TCPHGYKRLN STHCQDINEC TMPGVCQDGE CLNTQGSFLC ACKPGYILDR
TRCVEPPVEQ GQCFLMVTEA GQCKHALPTP LSQEMCCCTV GKAWGSKCER CPQDGTASFS
KICPAGKGYS YQTYSGSLII SPQMLQLYPN LEQLLHLSQT DGKHQEIKPQ PPQKEVPQVV
TTPTQTSTVS THRPQMPVIV AKPTPHPIIK VAPERDSLEV AQTQVTQTDE CRLNRNICGH
GDCINGQNGF TCQCHAGYRP HPQRKSCVDD NECESDPCGS GRGSCVNTMG SYRCRCLHGY
KLLVHQGKLK CVDVNECYKP HTCGEGGKCI NLPGSYKCEC FEGFKSRSHR QPVCEDINEC
RDPRTCPNGQ CENRPGSYEC VPCLPGHQAQ GGVCYDINEC QKRGVCPHGR CENLPGTYRC
LCKDGFLPGS DGRSCRDIDE CEDSRLCSNG RCLNTEGSFV CQCYSGYQRT KEGSHCEDIN
ECERSSKCLF GRCVNTMGSY RCECQNGFML VNGRRCQDID ECAMDRSLCQ PHGVCENRQG
AYICVCNEGY VSSEDKRGCE AIEVDIDNKK ECYLNLDDTV FCDSVLATNV TKQECCCSIG
VGWGDHCEIY PCPVYHSAEF HSLCPIGRGF YHEERMTEYG LAMRDIDECV LFSSEICKEG
RCMNTQPGYE CYCQQGFYYD SVLLECIDTD ECHDESLCTN GRCVNTRGSF YCMCSPPWVP
DTSKKKCVMP AVTGVNECQD PTNCRNGHCV DTPDTYYCIC TPPWILASDR NSCITPEEQG
DVNECEDPSY CQNGQCVNTP GSYHCICTQP HTFSAALKKC VYDDRTAAHK DVCFLQVDEG
LICSRPQKGL MVTYSECCCH YGRGWGPECR TCPQRNSGIF VRLCEMHLDT ESDGDVDSLA
AFVSYKPGGD SSEEDSDECS CTNGRCVPSY LGTVCECNPG FRLDHSRTRC TDIDECTEPG
LRINSCKNAR CINTLGSFKC YCKHGYVPTR RPNICVQART
//
