ID I7J4C9_CAEEL Unreviewed; 2656 AA.
AC I7J4C9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=EGF-like domain-containing protein {ECO:0000313|EMBL:CCJ09406.1};
GN Name=fbn-1 {ECO:0000313|EMBL:CCJ09406.1,
GN ECO:0000313|WormBase:ZK783.1g};
GN ORFNames=CELE_ZK783.1 {ECO:0000313|EMBL:CCJ09406.1}, ZK783.1
GN {ECO:0000313|WormBase:ZK783.1g};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCJ09406.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCJ09406.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCJ09406.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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; BX284603; CCJ09406.1; -; Genomic_DNA.
DR RefSeq; NP_001263716.1; NM_001276787.1.
DR EPD; I7J4C9; -.
DR EnsemblMetazoa; ZK783.1g.1; ZK783.1g.1; WBGene00022816.
DR GeneID; 176076; -.
DR AGR; WB:WBGene00022816; -.
DR WormBase; ZK783.1g; CE47732; WBGene00022816; fbn-1.
DR OrthoDB; 2881355at2759; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00022816; Expressed in embryo and 3 other cell types or tissues.
DR ExpressionAtlas; I7J4C9; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 12.
DR Gene3D; 2.10.25.10; Laminin; 17.
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; IPR024731; EGF_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001507; ZP_dom.
DR PANTHER; PTHR24039; FIBRILLIN-RELATED; 1.
DR PANTHER; PTHR24039:SF28; FIBULIN-1; 1.
DR Pfam; PF12947; EGF_3; 4.
DR Pfam; PF07645; EGF_CA; 8.
DR SMART; SM00181; EGF; 29.
DR SMART; SM00179; EGF_CA; 16.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57184; Growth factor receptor domain; 5.
DR PROSITE; PS00010; ASX_HYDROXYL; 9.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 16.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS01187; EGF_CA; 10.
DR PROSITE; PS51034; ZP_2; 1.
PE 1: Evidence at protein level;
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Proteomics identification {ECO:0007829|EPD:I7J4C9,
KW ECO:0007829|PeptideAtlas:I7J4C9};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..2656
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003710630"
FT TRANSMEM 2620..2640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 96..130
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 133..171
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 172..211
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 263..304
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 305..343
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 344..381
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1431..1472
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1473..1514
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1565..1603
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1606..1646
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1699..1740
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1838..1878
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1879..1919
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2129..2167
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2261..2301
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2312..2553
FT /note="ZP"
FT /evidence="ECO:0000259|PROSITE:PS51034"
FT REGION 669..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1929..1969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..879
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1014
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1937..1969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 99..109
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 120..129
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 371..380
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2656 AA; 279016 MW; 05E4E5E28AD90858 CRC64;
MSTRSRGSCS SPWFITPLVL LALCRGSHQI AKNFVNSSTP DLRPTFVVNF DTSTVICQHS
SDPTDLHIHN MSSLCDGKQD CFVNPAMHDE VFPYCEHKCQ STCSGKGACL YDGAKPQCYC
DSGFSGSACE LQDKNECLEH PCHMMAQCQN TLGSYECRCL PGYEGNGHEC TDIDECSDKL
TSRCPEHSKC INLPGTYYCN CTQGFTPKGN QGSGLDKCAD INECETGAHN CDADEICENS
IGSFKCVNKC SPGYELIDGK CEDVNECGSE KLHKCDVRAD CVNTIGGYEC ECEEGFEGDG
KNCQPKSSCR KNSAICDRHA SCHIVLDICD CKTGYTGDGI TCHDINECDA KDTPCSDGGR
CLNLDGGYVC CKNGQDDATC IKDQGAFCSG GCGDNAICSN ATCACIDGFR GDPHKKCVDI
NECVENDSVC GGVGDRCVNL FGGFKCCQHG STEAECTDQA FSSDSSTISS HGADFTTTGE
QIIEGSGSIQ TSSGGSITVT RGLIPKDVEL TTSGRLACTS YCPPNSECVG GYCECVSGYG
GNALVGCEDI DECITEICNI EANEWCVNLI GGFVCCNPTN ATHDDCIEIT KEKGLHVIGG
NEEDTVVATR SNHSTSDQLI TQVVQQSRNF STGQIILTRG KVSSGEAVTQ TTDADEFGLE
ISAADLAGSG SGITLPTTLE PKIEGSGKKA SGGVWTEEDE GEDEDLMEEG SGSWSTTING
TGITGSPRSE GTIRVRITTL GEDGEPETAT KPGISAPDKT GEGSKTESDG EEKLTVEKDG
KEAQSSGSSA TSSGKKSEAT SGSSSSSAKS GTGSEASGSS GASSSSGSGV SGESGSSVST
ESGSFGTSSS GSVGSEATGS TGVDGSESGK PSKSSTEEKL PFTKNGEKSP ISGSDTTGKE
SSEETTSRKP IEGSDSLTEG SGSGEWFETG SKGHFESGSK VSVTSGKGPT QSGAEGSGSG
PKVPKGPGAP EITTDGEESS STSTGDKSGG KPADKSDNKN VPKTGDKNPD ITTDGEDSTS
ETSGGEQGPK GKSKGQPPGD KGSEVKKPTS EVDGPGNLSG TKGKSNVPLK PTDLPEEGSG
ILTTSSGGKN STFEHGTKLE RLPPKTEDKS SETPQLGLEI SAGKKPEPED GTSKEVGLEI
LWESTTPGST TLDSDSVGLE ISGSDLTKAT KKPHVEIEGS GTGDEEITAT TRDVSKSTKK
PRVEVDGGDN GETSGVDGKP TTPAPTPSSS AESSTSRIPT TSEASPEGGS GEAGVPESPD
GSGESSTSAP DGVSPTSSAT APEVPTTSAS STPDAVEESG IPSTSKPTAE PLETTAPSTE
VTSPEGSGTE ESTLPPTEGS GESTTSSAPT VEPATVLPPQ NRNEKPEPTK DTFALPTTTT
GAPQANDSSV ENTKCTSSDE CGLDALCERR TGVCRCEPGF EGAPPKKSCV DVDECATGDH
NCHESARCQN YVGGYACFCP TGFRKADDGS CQDIDECTEH NSTCCGANAK CVNKPGTYSC
ECENGFLGDG YQCVPTTKKP CDSTQSSKSH CSESNMSCEV DTVDGSVECK ECMGGYKKSG
KVCEDINECV AEKAPCSLNA NCVNMNGTFS CSCKQGYRGD GFMCTDINEC DERHPCHPHA
ECTNLEGSFK CECHSGFEGD GIKKCTNPLE RSCEDVEKFC GRVDHVSCLS VRIYNGSLSS
VCECEPGFRF EKESNSCVDI DECEESRNNC DPASAVCVNT EGSYRCECAE GYEGEGGVCT
DIDECDRGMA GCDSMAMCIN RMGSCGCKCM AGYTGDGATC IKIEEEPKSD KTACTDEWSR
LCELEKKQCT VDEEEVPQCG ACLPGHHPIN GTCQSLQISG LCAQKNDCNK HAECIDIHPD
SHFCSCPDGF IGDGMICDDV DECNNAGMCD DENTKCENTI GSFNCVCLEG FKKVDEKCVV
DEKKQPNREK IEIDEENSSS SNSGQEKPTT KESLTTPQPP PTTTTTAKPA TTSASLCSTV
TCHSLATCEQ STGVCICRDG FIGDGTTACS KKSTADCISL PSLCADKAKC DNSTRSCECD
AGYIGDGYVC SPHPQDCVLR DNLCSPEAVC QNRRCQCLPG FTGDGVKCVS IHERASNCSQ
CDANAHCVGG TTCKCNPGYF GNGLCCVPDP LDCVHFTGIC HPNAVCNSES RQCQCSSGFS
GNGVSCFPQK SCRTDKSVCA KNAICLPTGS CICRHGFKGD PFYKCSSLVS KEPANQQDLS
DVSSCVTPCD SSTQLCISGE CICKSGFRRN STLSGSETCA DIDECAEKSH KCDRVATCRN
TFGSHVCTCP DGHVGDGITC VPHVNQGKLS VYCEADGMTL VLGNETADFE GKIFVKGQAE
NPYCSKSFSS LLNSRKPYVF KVVFQHCDVQ LLDNHTMAST VVVQKHAMFL TNKADSYDLR
CQYPIGSRAV ESHVNVSELA TTSTLTEKNS TLAPICRLSV SNDQHSSISS AMVGDTLKLA
LEVTPSENFG ILPRNCFAIN IESGERYTLT DDMGCAIDES LFPQWSAATS SKVQAVFRTF
KWPDSSMIRF QCDCNPCVGQ CSTPTCISSA RFRRHQTTSP VVNDEIRQEM VLMSGVESLA
VSSIINVHDS HDMNTSDDDD VTSSHVDATS KESKSICVKM APLLIALGSF AVCSAILLYL
CSKKPKTIDL ESELRF
//
