ID W5N9K1_LEPOC Unreviewed; 1196 AA.
AC W5N9K1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Fibulin 2 {ECO:0000313|Ensembl:ENSLOCP00000017310.1};
GN Name=FBLN2 {ECO:0000313|Ensembl:ENSLOCP00000017310.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000017310.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000017310.1}
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 EMBL; AHAT01015106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5N9K1; -.
DR Ensembl; ENSLOCT00000017341.1; ENSLOCP00000017310.1; ENSLOCG00000014039.1.
DR GeneTree; ENSGT00940000156047; -.
DR HOGENOM; CLU_268948_0_0_1; -.
DR Proteomes; UP000018468; Linkage group LG5.
DR Bgee; ENSLOCG00000014039; Expressed in larva and 13 other cell types or tissues.
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; 5.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24034:SF158; FIBULIN 2; 1.
DR Pfam; PF12662; cEGF; 2.
DR Pfam; PF07645; EGF_CA; 6.
DR SMART; SM00104; ANATO; 2.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00179; EGF_CA; 10.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 5.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 3.
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:UP000018468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1196
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004867455"
FT DOMAIN 870..908
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 913..954
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 955..993
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 994..1036
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 574..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1196 AA; 132896 MW; B3824623AF1A5C49 CRC64;
YKLRKSILFM TVLVLCISGA LCQKDCTGVD CPLLEHCIEE VLERGACCAS CLQKGCTCEG
YQYYDCINAG FRNGKVPEGE SYFVDFGSTE CSCPKGGGKI SCHFIPCPEV PPHCIEFSEP
SDGCLQCERF GCVHDGHKYD AGHTFQMDPC KVCHCPHAGG ELMCYPVPDC DLGTFQTPPL
FPTAHEENTS EKNNDELSNY ERAGSEDRLS QISHLPQSEK LPLFKTDIKD EDEDYDYTPT
DSAKSSLFDL AVPTKSAVTL VSYSDKPTAH EMFNEDLKQE LRQKIRTQEE ETKNEEITED
PLVGPTSQVF QDVRKSMEGI SGKGAEDYVT PHMAEEEHEE DEQVVTLKDV TEGGTDRKEV
TYVIDHELQT TETVPAVESN SHSSTTEENF LVQEDPLGKH GQAVLPTIKF SPTTQPPQIM
KAVEALISKK QSQTLYNYQQ KDAVQYTKFS GHLLVASCCE AGQKWASDNG HCTGMPQREV
NTCRIAEQQC CLGHLRDSKC LAGMTAAKEG KMCELGERDI CGADSYMECC SCCSLGLQFR
SEGHNCDSHQ HLVYPCSHMF LTCCEGEDGL SQPTLRERQK PEPTSLPKRV SDGTYDKEAF
SITDEEGNEN TVEKGEDIDE CLEYEGQLCH QRCINTRTSY ECACFPGYIL LSDGYSCEPE
NPEEEDNRLR EEDRPATPVP TVAASTTVIP VDLCAGNGPC MHVCSQAAGE VLCSCFPGYA
LMADGHSCED INECLTNTHS CQAMERCINT IGSFTCEKQI TCSPGYQLKE DTCEDIDECL
QQTHNCGTGF ECQNTAGSFY CNPKHRCFTG FSQDQHGNCI ADIDECSSPN VPCSPGFNCI
NTVGSYTCQR KIIVCSRGYH ASPDGARCID VDECQTGVHR CGEGQICHNL PGTYRCDCKT
GYQYDMFRKV CVDVNECWRY PGRLCAQTCE NTPGSYQCSC TTGFTLSSDG KNCEDVNECE
KNPCSQECAN IYGSYQCYCR QGFYLKEDGH SCEDIDECSQ SVGNLCAFQC VNVPGSYQCA
CPAHGYTMSP NGRTCRDIDE CAVGTHNCST AETCYNIQGG FRCLSFSCPP NYRRVSDTRC
ERLSCPNYVE CQSSPLRITY YHLSFQTNIV IPAQIFRIGP SPAYSGDNII ISITRGNEEN
YFSARKLNSY TGAVYLQRQV REPKDFLIDV EMKLWRQGNF TTFLARIYVF ITAPSL
//
