ID A0A2Y9REL8_TRIMA Unreviewed; 1426 AA.
AC A0A2Y9REL8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Latent-transforming growth factor beta-binding protein 1 isoform X7 {ECO:0000313|RefSeq:XP_023591906.1};
GN Name=LOC101345588 {ECO:0000313|RefSeq:XP_023591906.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023591906.1};
RN [1] {ECO:0000313|RefSeq:XP_023591906.1}
RP IDENTIFICATION.
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_023591906.1; XM_023736138.1.
DR Proteomes; UP000248480; Unplaced.
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; 16.
DR Gene3D; 3.90.290.10; TGF-beta binding (TB) domain; 4.
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; PF07645; EGF_CA; 14.
DR Pfam; PF12661; hEGF; 1.
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; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 10.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 8.
DR PROSITE; PS50026; EGF_3; 10.
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:UP000248480};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 201..233
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 359..400
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 428..465
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 479..525
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 664..705
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 787..827
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 828..868
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 869..909
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 910..950
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 951..992
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1052..1106
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1229..1282
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1326..1362
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1367..1411
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 33..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 205..215
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 223..232
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1426 AA; 155992 MW; C0E1E4F31ED04210 CRC64;
MCLRPQLCVC KPGTKGKACE TTATQDTLSI AVSGGQSPGA ASNWIPPEPA SKHTPSKKAD
TLPRISPVAQ MTLTLKPKPS VGLSQQIHSQ VTPLSSQNVM VHHGQTQEYV IKPKYFPAQK
VISGEQSAEG LLPLRYGQDP GTAPFQSSNH TGRIKVVFTP SICKVTCTKG SCQNSCEKGN
TTTLISENGH AADTLTATNF RVVICHLPCM NGGQCSSRDK CQCPPNFTGK LCQIPVHGAN
VPKLYQHSQQ SGKALGTHVV HSTHTLPLTM TNQQGVKVKF PPNIVNIHVK HPPEASVQIH
QVSRIDDPTG QKVKETQPGQ SQVSYQGLPI QKTQTVHSTY SHQQVIPHIY PVAAKTQLGR
CFQETIGSQC GKPLPGLSKQ EDCCGTVGTS WGFNKCQKCP KKPAYHGYNQ MMECLQGYKR
VNNTFCQDIN ECQLQGVCPN GECLNTMGSY RCTCKMGFGP DPTFSSCIPD TPMISEEKGP
CYRLVSSGRQ CMHPLSVHLT KQLCCCSVGK AWGPHCEKCP LPGTAKEEPV EALTFSQEHG
PGVAEPEVAT APPEKEIPSL DQEKTKLEPG QLQLSPGVST VHLHPQFPVV IEETSPPVPV
EVAPEASTSS ARQVIAPTQV TEINECTVNP DICGAGHCIN LPVRYTCICY EGYKFIEQQR
KCVDIDECTQ VQQLCSQGHC ENTEGSFLCI CPAGFMASEE GSNCLDVDEC LRPDVCGEGH
CVNTMGTFQC EYCDSGYRMT RTGNCEDINE CLTPSTCPDE QCVNSPGSYQ CIPCTEGFRG
WNGQCLDVDE CLEPNVCVNG TCFNLEGSYM CSCHQGYSPT LDRKHCKDID ECQQGNLCIS
GQCKNTEGSF RCTCGQGYQL SAAKDQCEDI DECQHHRLCT NGQCRNMEGS FQCVCDQGYR
ASALGDHCED INECLENNHI CLGGDCVNTA GSYDCTCPNG FQLNDSKRCQ DINECEQPGL
CGPHGECLNT DGSFQCVCEQ GFSISADGPT CEDVNECELL SGVCGEAFCE NVEGSFLCVC
ADENQEYSPM TGQCRSQASE DLDVDQPKEE KKECYYNLND ASLCDNVLAP NVTKQECCCT
SGAGWGDNCE IFPCPVSGTA EFTEMCPRGK GFVPTGESTH GVGGQNYKDA DECSLFGQEI
CKNGFCLNTQ PGYECYCKQG TYYDPVKLQC FDIDECQDPS SCIDGQCINT EGSYNCFCTH
PMVLDASEKR CIQPAESNEQ IEETDVYQDL CWEHLSDEYV CSRPLVGKQT TYTECCCLYG
EAWGMQCALC PMKDSDDYAQ LCNIPVTGHR QPYGRDALVD FSEQYAPEAN PYFIQDRFLN
SFEELQAEEC GILNGCENGR CVRVQEGYTC DCFDGYHLDM AQMTCVDVNE CDELNNRMSL
CKNAKCINTE GSYKCLCLPG YVPSDKPNYC TPLNTAMNLE KDSDLE
//
