ID A0A0V0UQ30_9BILA Unreviewed; 885 AA.
AC A0A0V0UQ30;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Fibulin-1 {ECO:0000256|ARBA:ARBA00021554, ECO:0000256|PIRNR:PIRNR036313};
GN ORFNames=T09_7110 {ECO:0000313|EMBL:KRX53423.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX53423.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX53423.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX53423.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homomultimerizes and interacts with various extracellular
CC matrix components. {ECO:0000256|PIRNR:PIRNR036313}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|PIRNR:PIRNR036313}.
CC -!- SIMILARITY: Belongs to the fibulin family.
CC {ECO:0000256|ARBA:ARBA00006127, ECO:0000256|PIRNR:PIRNR036313}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX53423.1}.
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DR EMBL; JYDN01000202; KRX53423.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0UQ30; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016504; F:peptidase activator activity; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 6.
DR Gene3D; 2.10.25.10; Laminin; 10.
DR InterPro; IPR000020; Anaphylatoxin/fibulin.
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; IPR017048; Fibulin-1.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24034:SF46; LATENT-TRANSFORMING GROWTH FACTOR BETA-BINDING PROTEIN 3; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 6.
DR PIRSF; PIRSF036313; Fibulin-1; 3.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00179; EGF_CA; 8.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 5.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530,
KW ECO:0000256|PIRNR:PIRNR036313};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR036313};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..885
FT /note="Fibulin-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006870181"
FT DOMAIN 398..440
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 441..484
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 485..525
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 526..570
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
SQ SEQUENCE 885 AA; 98709 MW; 91DDA6142DBCD7BB CRC64;
MSNLPMLNLL LLLLLFYQPH VVEANQSSLA ECCLEGKKAY AISKQCTKTT VEKIDQAGFC
PRVASICCLV AFYETKCSEG KSIALAGDSC EALDAPGREQ TKECCECCSL AKEMKKQGKQ
CNAPVDFSAN CKAVFDQCCR YESAASRDEQ SNLQTDFAEF TASVSSTTVG LDLSEQCDEE
EEKFCEQQCR RVPGQKSISC SCRAGYMLNA DGRTCSDVNE CEENPPPCDV VSQICENTIG
SFRCSCMNGF AWNETTNLCV DIDECLLFRD NCIAGQRCIN TIGSWRCIRT MSCGTGYYLD
SESDSCVDID ECALGTHNCG PGFTCRNTHG SFRCERRFCP SGQQWNSTAK RCVTISGCSH
GFYLASDGSC QGSYYCKDLP RACAPGYQLN PVTSVCEDID ECMKGTHTCP NVESCVNSIG
GYHCECRSGF RFNSVIKKCE DINECQNRSS VLCSTHGSCV NTVGSFHCVC DPGYELSSDG
RQCVDVDECR TGTAQCEHRC VNIPGSYQCV CERGYSLGVD GRSCVDIDEC KMWNTQGTAM
CMGKCINTAG SFRCECPPGF RLNSDSRTCE DIDECQQGLC SKDDDICVNL YGGYRCHQII
CPQNYQRDLR FKNRCTRKTL FCLPSDRDCM NAPMSILYNF IALTNELRFQ DFGMNALPLI
TFNGPVNAET SVQYELQLDR VVTLGSKTVK PATRASFSVQ KLITKPNAAV LNLIEPLQGP
QQVDLDLIMH FRHAGNFGGR SLSKIVLHVS EYKENHFSFS VRDGYTCWKK CNPLDIGCLA
NRTYSISYQF IALPEMSPRL KGPLEISRVY PEQASHRRWP LRVQYSIIDN PSRRYDVQQQ
DNTGIIYMKY PITKKTNEMI QLEMKIYSST NVLTEQNYAY ISVFS
//
