ID A0A1S3I7E6_LINUN Unreviewed; 1230 AA.
AC A0A1S3I7E6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Fibrillin-2 {ECO:0000313|RefSeq:XP_013393294.1};
GN Name=LOC106161014 {ECO:0000313|RefSeq:XP_013393294.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013393294.1};
RN [1] {ECO:0000313|RefSeq:XP_013393294.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013393294.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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_013393294.1; XM_013537840.2.
DR AlphaFoldDB; A0A1S3I7E6; -.
DR STRING; 7574.A0A1S3I7E6; -.
DR EnsemblMetazoa; XM_013537840.2; XP_013393294.1; LOC106161014.
DR GeneID; 106161014; -.
DR KEGG; lak:106161014; -.
DR InParanoid; A0A1S3I7E6; -.
DR OrthoDB; 354414at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.25.10; Laminin; 20.
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:SF166; VACUOLAR-SORTING RECEPTOR 1; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF14670; FXa_inhibition; 17.
DR PRINTS; PR00907; THRMBOMODULN.
DR SMART; SM00181; EGF; 20.
DR SMART; SM00179; EGF_CA; 20.
DR SUPFAM; SSF57184; Growth factor receptor domain; 7.
DR PROSITE; PS00010; ASX_HYDROXYL; 18.
DR PROSITE; PS01186; EGF_2; 17.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS01187; EGF_CA; 6.
PE 4: Predicted;
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1151..1175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..97
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 98..138
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 139..179
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 262..303
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 304..344
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 345..385
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 386..426
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 509..550
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 551..591
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 592..632
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 633..673
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 674..714
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 715..755
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 756..796
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 797..837
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 864..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1230 AA; 132596 MW; 652F1030798CBCF7 CRC64;
MASFQVPRSK LFHFIDINEC AVNNGGCSGR CTNANGSHTC TGGCKKGYTP RGNRCTDINE
CSNKKGGCSD TCINLPGSYN CSCGKGYTLG TDAKTCKDVD ECKTNNGGCS QICKNRPGSF
KCSCRTGYSL ASDKKRCNDN DECSNKNGGC QHTCHNTPGS FTCACKRGFV LSSDGKTCSD
IDECRFQKGN CSQTCSNTVG SFRCGCRTGY ALAADKRTCT DVNECRNKNG GCSHNCSNTM
GSFKCSCREG YSLSGDKRSC KDVNECNNSN GGCSHQCNNF PGSYNCSCPD GYNLLNNNKK
TCEDVDECSS GNGGCSYKCK NYPGSYNCSC PDGYELNIDK KTCKDIDECR SNNGGCSHTC
QNQAGTYACS CPAGYNLLKD LKNCQDIDEC SVENGGCSHT CHNYQGSYNC SCPDGYNLLK
DRKNCQDIDE CRFQKGNCSQ TCSNTAGSFR CGCRTGYALA ADKRTCTDVN ECRNKNGGCS
HNCSNTMGSF KCSCREGYSL SGDKRSCKDV NECNNSNGGC SHQCNNFPGS YNCSCPDGYN
LLNNNKKTCE NVDECSSGNG GCSYKCKNYP GSYNCSCPDG YELNIDKKTC KDINECRSNN
GGCSHTCQNQ AGTYACSCPA GYNLLKDLKN CQDIDECSVE NGGCSHTCHN YQGSYNCSCH
DGYKLLKDGK NCEDIDECSF KNGGCSHTCH NYQGSYNCSC PDGYNLLKDE KNCQDINECS
VKNGGCSHTC HNYQGSYNCS CPDGYNLLKD RKNCQDIDEC SVENGGCSHT CHNYQGSYNC
GCPDGYNLLK DGKNCQDVNE CNKNNGGCSH TCHNYQGSYN CSCPDGYTMR KDEKSCEAVP
TTEAQKTTST ETITSEHVPI VTPEATTQTK KTLAPETKPS PKSNPAVPIS TTEYFISETS
TGEKTSTTLS VPSQTNDILV TKTTSVKITS AASPVYTYTS EALTAKTTAV KSQSVTSRMP
AKTNEALSTK SSTLSGKTTV SSQYTQSVLA VSTETVVGLT TPSVERTTLP SGPVTKLNPV
TKLNVETTLT PAHITSSAKQ LTTAGGFQST KAIERLSTDR TKYTTTSTRR ETTAVPKVQT
SKESTEQTTE FIEVTTTSLG AKNTKSVDKT DAPKDSTKAA MNTNPVTKPS DLPSISDKRQ
AERQAQQQET YTYAGVGVGA GVIIIVITAI SAFMIKRRRV GKGPDRLYFD DLDDNISQPE
ENSDKAFENP TYCDVLNLSQ DGMIDIDLDA
//
