ID A0A3B4B4Y7_9GOBI Unreviewed; 1253 AA.
AC A0A3B4B4Y7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Latent transforming growth factor beta binding protein 2 {ECO:0008006|Google:ProtNLM};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000023626.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000023626.1}
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; A0A3B4B4Y7; -.
DR STRING; 409849.ENSPMGP00000023626; -.
DR Ensembl; ENSPMGT00000025173.1; ENSPMGP00000023626.1; ENSPMGG00000019100.1.
DR Proteomes; UP000261520; 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; 15.
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; 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; 2.
DR Pfam; PF07645; EGF_CA; 10.
DR Pfam; PF00683; TB; 4.
DR SMART; SM00181; EGF; 16.
DR SMART; SM00179; EGF_CA; 15.
DR SUPFAM; SSF57196; EGF/Laminin; 9.
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; 8.
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, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1253
FT /note="Latent transforming growth factor beta binding
FT protein 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017280199"
FT DOMAIN 73..105
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 207..248
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 277..317
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 327..379
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 478..517
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 518..558
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 725..764
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 765..806
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 807..849
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 903..946
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1082..1135
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1192..1236
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 106..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..459
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 77..87
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 95..104
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1253 AA; 137266 MW; FAF19FAD1FF11FD5 CRC64;
KPIPLMCLAC FVFVLPYWLS VGLDRIKIIF TPMLCRRVCS SGRCYNSCEK GDTTTVYSEN
PHYSLLCLSL FLFAVFCQIP CQNGGRCIGR DHCWCPSNST GKFCHLPSPP PPPRPSPPST
KDTTSLHPSI VNVHIQHPPE AEVQVHQVAR VQPGQRPPVA EGAHSVQQRS QPSNGHEPTN
EHTDRQHHNN DQTPHRPHPY PNGNGVGRCF QETVDGQCGK PLPGLTKKDD CCGSVGASWG
LNKCQKCPAK PAYAVIANGQ VECSKGYKRL NLTHCQDINE CTLPGICKNA DCLNTKGSYR
CTCKPGFMLD PARSHCISDK AVSDQRGMCY RSLSARTCSL PLSQHITKQI CCCSRVGKAW
GHACERCPLP GSDHFKEICP VGHGYTYSRS DVQISLRQLD DDELQSTGLS WEEESPTYPQ
LPSFDPSLPH LHPSHPDTPH RPQHPVYPQT PHVPRQPVTP HLPYPPFVDN NTPRETDDVN
ECLNQTACSH GRCVNTEGSY RCNCFQGYKL SSDNSCQDVD ECVRPGVCLY GRCSNLDGSY
KCSCNHGYKV TSDGKACEDV NECAAGNACP AGICLNTVGS FTCQKCRPGF GPSCSLFPDV
DECAQGDVCH GGICANTEGS YTCTRCKAGY SVSSDRRRCE DIDECRSLST CANGICLNTE
GSYTCENCPS GYTVSYDGEL CEDIDECRLP HTCPQGRCTN THGSFTCLEC QPGFRVSDDG
LQCDDLNECD DPQKCSGGLC TNTIGSFSCS CPSGSELVYG TSCQDIDECS RVVGLCGEGR
CQNTPGSYVC LCPDGYTTEE GRSGCQDIDE CLNETICGNN GMCENTDGSF RCQCDQGYTN
PPGDMTRCVD VNECEMSEAR CGEALCENHD GSFLCFCPSA NEEFDPISSQ GSLDLAVSIP
ERKECYYNLN DANFCDNVLS RNVTKQECCC TVGAGWGDNC EIHACPVLGR GMTDLLFTLL
CPHGSGLLSV SVSKVQALGD RHANECEMFG PDICKNGQCS NLFSTYTCYC RSGFYYDNIR
LECVDYDECE LGNMCVDGVC VNTAGSFNCF CSPPLVLDST RRRCISLNTT EIAEPDHDVH
MDICWQRLEG DNMCSEPLQG QRTTYTECCC LFGVAWSGQC AFCPRKDSED YAIMCNLPRR
GERYEGFEGL RAEECGVLNG CENGRCVRVR EGYTCDCFDG YELNLNKMAC IDINECEDIS
DKVPLCQNGL CSNTEGSYKC TCLPGFVASA QPHKCIPAIP ERPTATDKRK DGD
//
