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Database: UniProt
Entry: A0A2Y9JMF4_ENHLU
LinkDB: A0A2Y9JMF4_ENHLU
Original site: A0A2Y9JMF4_ENHLU 
ID   A0A2Y9JMF4_ENHLU        Unreviewed;      1302 AA.
AC   A0A2Y9JMF4;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Latent-transforming growth factor beta-binding protein 3 isoform X1 {ECO:0000313|RefSeq:XP_022362137.1};
GN   Name=LOC111149403 {ECO:0000313|RefSeq:XP_022362137.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022362137.1};
RN   [1] {ECO:0000313|RefSeq:XP_022362137.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022362137.1};
RG   RefSeq;
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   RefSeq; XP_022362137.1; XM_022506429.1.
DR   STRING; 391180.A0A2Y9JMF4; -.
DR   KEGG; elk:111149403; -.
DR   OrthoDB; 354414at2759; -.
DR   Proteomes; UP000248482; Unplaced.
DR   GO; GO:0031012; C:extracellular matrix; IEA:UniProt.
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; 11.
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; 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:SF43; LATENT-TRANSFORMING GROWTH FACTOR BETA-BINDING PROTEIN 4; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF07645; EGF_CA; 10.
DR   Pfam; PF12661; hEGF; 3.
DR   Pfam; PF00683; TB; 4.
DR   SMART; SM00181; EGF; 15.
DR   SMART; SM00179; EGF_CA; 14.
DR   SUPFAM; SSF57196; EGF/Laminin; 6.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR   SUPFAM; SSF57581; TB module/8-cys domain; 4.
DR   PROSITE; PS00010; ASX_HYDROXYL; 9.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 11.
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:UP000248482};
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..39
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           40..1302
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015969326"
FT   DOMAIN          108..140
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          276..319
FT                   /note="TB"
FT                   /evidence="ECO:0000259|PROSITE:PS51364"
FT   DOMAIN          354..394
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          402..454
FT                   /note="TB"
FT                   /evidence="ECO:0000259|PROSITE:PS51364"
FT   DOMAIN          573..614
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          615..652
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          659..701
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          743..783
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          784..824
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          825..864
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          865..907
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          916..970
FT                   /note="TB"
FT                   /evidence="ECO:0000259|PROSITE:PS51364"
FT   DOMAIN          1035..1075
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1081..1121
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1135..1185
FT                   /note="TB"
FT                   /evidence="ECO:0000259|PROSITE:PS51364"
FT   REGION          245..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1187..1216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..271
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..514
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        112..122
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        130..139
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1302 AA;  138949 MW;  27F967CAC54D384E CRC64;
     MPGPRGAAGG LAPEMRGAGA AGLLALLLLL LLPLGPGGGA EGGPAGERGA GGGGALARER
     FKVVFAPVIC KRTCLKGQCR DSCQQGSNMT LIGENGHSTD TLTGSGFRVV VCPLPCMNGG
     QCSSRNQCLC PPDFTGRFCQ VPAGGAGGGT GGSGPGLGRA GTLSTGALPP LAPESESVAS
     KHAIYAVQVI ADPPGPGEGP PAQHAAFLVP LGPGQISAEV QAPPPVVNVR VHHPPEASVQ
     VHRIEGPNAE GPAPSQHLLP HPKPQHPRPP TQKPLGRCFQ DTLPKQPCGS NPLPGLTKQE
     DCCGSIGTAW GQSKCHKCPQ LQYTGVQKPG PLRGEVGADC PLGYKRLNST HCQDINECAM
     PGMCRHGDCL NNPGSYRCVC PPGHSLGPSR TQCIADKPEE KSLCFRLVSP EHQCQHPLAT
     RLTRQLCCCS VGKAWGARCQ RCPADGTAAF KEICPAGKGY HILTSHQTLT IQGESDFSLF
     LHPDGPPKPQ QLPESPSRAP PPEDTEEERG VSTDSPVVEE QSAAQSHPTA TTSPARPYPE
     LISRPSPPTV RWFLPDLPPS RSAVEIAPTQ VTETDECRLN QNICGHGECV PGPSDYSCHC
     NPGYRSHPQH RYCVDVNECE AEPCGAGRGV CMNTGGSYNC HCNRGYRLHV GAGGRSCVDL
     NECAKPHLCG DGGFCLNFPG HYKCNCYPGY RLKASRPPVC EDIDECRDPS SCPDSKCENK
     PGSFKCIACQ PGYRSQGGGA CRDVNECAEG SPCSPGWCEN LPGSFRCTCA QGYAPAPDGR
     SCQDVDECEA EDVCDNGICT NTPGSFQCQC LSGYHLSRDR SRCEDIDECD FPAACIGGDC
     INTNGSYRCL CPQGHRLVGG RKCQDIDECS QDPGLCLPHG ACENLQGSYA CICDEGFTPT
     QDHHGCEEVE PPHHKKECYL NFDDTVFCDS VLATNVTQQE CCCSLGAGWG DHCEIYPCPV
     YSSAEFHSLC PDGKGYTQDN NIVNYGIPAH RDIDECILFG AEICKEGKCV NTQPGYECYC
     KQGFYYDGNL LECVDVDECL DESNCRNGVC ENTRGGYRCA CTPPAEYSPA QRQCLSPEEM
     DVDECQDPAA CRPGRCVNLP GSYRCECRPP WVPGPSGRDC QLPESPAERA PELRDVCWAQ
     RGEDGMCAGP LAGPTLTFDD CCCRQGRGWG AQCRPCPPRS SGSQCPTSQS ESNSFWDASP
     LLLGKPPREE DSSEEDSDEC RCVSGRCVPR PGGAVCECPG GFQLDASRAR CVDIDECREL
     NQRGLLCKSE RCVNTSGSFR CVCKAGFARS RPHGACVPQR RR
//
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