ID A0A096M2Z0_POEFO Unreviewed; 997 AA.
AC A0A096M2Z0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=EGF like, fibronectin type III and laminin G domains {ECO:0000313|Ensembl:ENSPFOP00000025781.1};
GN Name=EGFLAM {ECO:0000313|Ensembl:ENSPFOP00000025781.1};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000025781.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000025781.1}
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 EMBL; AYCK01002920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01002921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A096M2Z0; -.
DR Ensembl; ENSPFOT00000025596.1; ENSPFOP00000025781.1; ENSPFOG00000018544.2.
DR GeneTree; ENSGT00940000158504; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProt.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
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; 2.
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; 2.
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:UP000028760}.
FT DOMAIN 38..138
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 146..241
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 332..370
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 375..553
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 554..591
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 600..777
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 773..809
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 816..995
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 282..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 341..358
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 360..369
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 581..590
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 799..808
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 968..995
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 997 AA; 109426 MW; 192614ACAC6693DB CRC64;
LEAKSCSALS SLVFTQSLQF ESLSFTTCLK TESKVGNPPL DIQLETLNCS AFSVRWKMPR
RHVSTITGYK VFYTEMKNGR PVSTTSIMEV PLSLDMLTTD VNIGNLKMNS KYRVSVGAYG
WAGEGRPSMP RDISTASHEM CMPPSPPTQP IVMAVSDTEL ALSWQEGESE GSSPVLHFLV
AYIRPEMDTE WTYIREPIET SSMVLKGLLP ETEYQFVVRA VNIYGVSPPS HINNPVRTLG
SLEMGSGDVG RYNTDPRYKD EDGFDIDDSD YDVFIEELKP FPGIGENNVP SERSSTTDTP
TTAPSTTTSP PSATTASICT ISPWKGEIPR VYDLACDDTV CPPDSFCLTD YESGGSRCHC
NLGRRGDSCS EAVTVNFPRF YGYSHMTFEP LKNSYQTFQI TLEFKADSED GLLLYCGENE
HGRGDFTSLA LVQGKLHYRF NCGTGAAQII SESPVVLGQW HIVTIFRDGM SGWLRMDNDN
PISGRSLGQY TKITFRSPLY VGGSPGAYWL VRATGTNRGF VGCIQSLTIN NKATDIRPWP
LGKALSGADI GECSDRVCDM VSCANGGVCF ANRADGYICL CPLGFKGALC EESFSLSSPL
FNETVFSYAV IRWPQSSQSY LSFMEFEVTF WPSAPSGVLL YSDDAGSRDF LAINLVDRYL
EFRFDCGSGE AVIRSEEQIN LDSWHELRVS RTAKSGILQV DNQKPMEGIA EGAFTQINCS
SPLYLGGVPD YEKTKRTAGV MKPFTGIIQK LILNDRAMPI TAGSAGGVNI ANSAHPCVEN
PCANGGTCRP KWDDYECDCP LGYDGRHCQK AVTEAIEIPQ FIGRSYLTYD NRDILKRVSG
SRTNLFMHFK STAKDGLLLW RGDSPMRPNS DFISMGLQDG ALIFSYNLGS GMANIVVNGT
FSDGKWHRVK AVRDGQSGKL TVDDYGAKTG RSPGKMRQLN INGPLYVGGM KEIALHTNRQ
YLGGLVGCVS HFTLSTDFHL ALVEDAADGK NINTCSN
//
