ID A0A3Q3NGE3_9TELE Unreviewed; 1304 AA.
AC A0A3Q3NGE3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Fibulin 2 {ECO:0000313|Ensembl:ENSMAMP00000035136.1};
GN Name=FBLN2 {ECO:0000313|Ensembl:ENSMAMP00000035136.1};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000035136.1, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000035136.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the fibulin family.
CC {ECO:0000256|ARBA:ARBA00006127}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR Ensembl; ENSMAMT00000036040.2; ENSMAMP00000035136.1; ENSMAMG00000023589.2.
DR GeneTree; ENSGT00940000156047; -.
DR Proteomes; UP000261640; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; 7.
DR Gene3D; 2.10.25.10; Laminin; 9.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24034:SF194; NIDOGEN (BASEMENT MEMBRANE PROTEIN); 1.
DR Pfam; PF12662; cEGF; 3.
DR Pfam; PF07645; EGF_CA; 4.
DR SMART; SM00104; ANATO; 2.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 9.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 4.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 4.
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}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1304
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018529465"
FT DOMAIN 606..642
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS01178"
FT DOMAIN 683..715
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS01178"
FT DOMAIN 768..809
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 977..1015
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1020..1061
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1062..1100
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 212..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1304 AA; 144403 MW; 979B443715041EE2 CRC64;
MACLIRAEVA FLSGTLLLLY LSACLCQRDC TGVDCPLLDN CIEEVLESGS CCASCLQKGC
TCEGYQYYDC INAGFKNGKV PEGDSYFVDY GSTECSCPMG GGRISCHFIS CPEMPPNCIE
VSEPADGCMQ CERVGCDHGG QKYEAGHSFH INPCRVCHCP NEGGELMCYP VPDCDPNKVH
KPVLAESTDE DTANRHDSYP YRFDQQAHTD QFPTQYHLPP DGNVSLFKSS PLDKEDPEDY
DYGPTDLPET YPHSLLFPTQ SSSSNKVISK SRGSDKPDRT SAFQSFDRRG KLELKEQYAV
HDKAEVTENP LGKEQSSVRP HIHEVATTSW QPSHGPTSVQ SVSFTEQSPQ TALENPRHAH
SSVIFPLHKG LGEEKQSEYT HMFSESTVHN SVSKTHHQNA SDNVIHRGRG KNTQISVSHQ
GRGTESQSNL QTQSDIMNSN GKKELAGTAI PEREEGVEAE DMEEGKQEEE NVTFQSVTEP
EGKAVPYMIK SAQQERNHKE SESSDPTSSY DETTSESSTN SPGHSENHTA TIVHFITTTT
QPPVRVKLDE SQPSRRPGQS LFNLRSEDRE EMKEEVTKKE EKRKDRPVFL IKLDGGVSGD
DLLLNCCTAG QRWATENHHC NHMPMLNNDK YSKCSVAQKQ CCLSSVKESQ CGSGVTSARG
GGTCEMDRKD HCSDDSYQVC CSCCALGLQM RREGQSCDAH QYLGYPCGHV FLTCCEEEEG
PSQIPLKRKQ KPKPTYMPRQ VSDSKFPKEA FSISTTDEAT NAVEEQDDVD ECQLYAGQLC
QHTCTNVWGS YRCDCHQGYI LQQDRHTCAP VSPDEDNRVR EESPAVVPTQ ATTNSTTTTS
PSRLKPCAEN SPCSQQCKVV AGQAHCSCFP GFSLMTDGHM CEDIDECVLQ THNCGMGFTC
ENTVGSFLCN SKHKCIRGFT QDSHGNCIDI NECSSLTEPC SSGFNCINTV GSYTCQQKNI
MCGQGYHTSP DGAKCIDIDE CQMGTHRCGV GQICHNLPGS YRCDCQTGYQ YDAFRKACTD
VNECWRYPGR LCAQTCENTP GSYHCSCTAG FSLALDGKNC EDINECDKNP CSQECANIYG
SYQCYCRQGY FLKEDGHTCE DIDECSQSIG TLCAFKCVNV AGSYQCSCPP HGYIMSTNGH
TCTDIDECTA GTHNCPYGQT CYNLQGGFRC LSFDCPHNYK KVSDTRCERI SCPSNSIDCQ
NSPVRITYYQ LSFQTNIIIP AQIFRIGPSP AYSGDHIIIG ITKGNEEGYF STRKLNSFTG
GVYLQRQVRK PKDFLIDVEM KLLRQGTFTS FLARIYVFIT SSTM
//