ID U3JH70_FICAL Unreviewed; 964 AA.
AC U3JH70;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=EGF like, fibronectin type III and laminin G domains {ECO:0000313|Ensembl:ENSFALP00000002124.1};
GN Name=EGFLAM {ECO:0000313|Ensembl:ENSFALP00000002124.1};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000002124.1, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000002124.1, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000002124.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; U3JH70; -.
DR STRING; 59894.ENSFALP00000002124; -.
DR Ensembl; ENSFALT00000002136.2; ENSFALP00000002124.1; ENSFALG00000002044.2.
DR eggNOG; KOG0613; Eukaryota.
DR eggNOG; KOG3509; Eukaryota.
DR GeneTree; ENSGT00940000158504; -.
DR HOGENOM; CLU_013380_0_0_1; -.
DR OMA; CGEGTIE; -.
DR Proteomes; UP000016665; Chromosome Z.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005614; C:interstitial matrix; IEA:Ensembl.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005539; F:glycosaminoglycan binding; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001791; Laminin_G.
DR PANTHER; PTHR15036:SF88; PIKACHURIN; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00054; Laminin_G_1; 2.
DR Pfam; PF02210; Laminin_G_2; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
PE 4: Predicted;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
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}; Reference proteome {ECO:0000313|Proteomes:UP000016665}.
FT DOMAIN 1..89
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 97..192
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 298..336
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 341..519
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 520..557
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 564..743
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 739..775
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 782..961
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 263..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 307..324
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 326..335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 547..556
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 765..774
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 934..961
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 964 AA; 105267 MW; 1DFF8ADDE5F4CA0C CRC64;
MPKQHASTIT GYTVFYSEVE GDKAVKQLSH DVPLSLDMIS MGQPEGQAIF DVVIGDLKPG
TRHRVSVGAY GWAGKGRPSM PRDVTTLSQD KCMPPVPPSQ PQVVVVSDSE VALSWKPGVS
EGSSAIQYYT VEFIRPDLDS NWTGIREQIQ MESMVLKGLL PNTKYQFAVR AANSFGSSPA
SAPSDVIRTF GSEELGSGSY GHRYITDTVT GDGDGFDIDD SDYDIYIEEL RPLPAIKGGN
RKFLVETKVT PGSSSRLLSR VLTTTSEPTA SPPTTSGPAP ARAWAARRGS MSSAARLLEL
SCDEAVCSAD SFCINDYDRG GSRCHCNLGR GGDTCEEDIS IQYPQFSGYS YITFEPLKKS
YQTFQITLEF RAESEDGLLL YCGENEHGRG DFMSLAIIRH SLQFRFNCGT GAGVITSENK
IKLGNWHSVT LFRDGVNGWL RMDSNAPVTG KSQGQYSKIT FQTPFYVGGA PSVYWLVRAT
GTNRGFQGCV QSLSINGRRI DMRPWPLGKA LSGADVGECS SGICDEAACI NSGTCTASKA
DSYICLCPLG FKGHHCEEAL TLAIPQFNES LRSFASTPWP LEPQNYLSFM EFELTFRPDL
ETGVLLYSYD TDSKDFLSIN MVAGYVEFRF DCGSGTAVIR SEEPVSLGQW HELRVSRTAK
NGILQVDKQK PVEGMAEGAF TQIKCSSEIF IGGVPNYDDV KKNSGILRPF SGSIQKIILN
DRTIDVKQDF TFGINLANAA HPCVTSPCAN GGTCVPKKES YECDCPLGFD GQHCQKAITE
AIEIPQFIGR SYLTYDNPDI LKRVSGTRTN VFMRFKTTMK EGLLMWRGNS PMRPNSDFIS
LGLQEGALIF SYNLGSGIAA ITVNGSFSDG RWHRVKAVRD GQSGKVTVDD YGARTGKSPG
KMRQLNINGD LYVGGMKEIA LHTNRQYLRG LVGCISHLTL STDYHISLVE DAANGKNINT
CGTK
//
