EGFL6_XENLA
ID EGFL6_XENLA Reviewed; 544 AA.
AC Q8AVH7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Epidermal growth factor-like protein 6;
DE Short=EGF-like protein 6;
DE Flags: Precursor;
GN Name=egfl6;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in organ morphogenesis. Promotes matrix
CC assembly (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nephronectin family. {ECO:0000305}.
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DR EMBL; BC042275; AAH42275.1; -; mRNA.
DR RefSeq; NP_001080354.1; NM_001086885.1.
DR AlphaFoldDB; Q8AVH7; -.
DR SMR; Q8AVH7; -.
DR DNASU; 380046; -.
DR GeneID; 380046; -.
DR KEGG; xla:380046; -.
DR CTD; 380046; -.
DR Xenbase; XB-GENE-983967; egfl6.S.
DR OrthoDB; 766075at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 380046; Expressed in lung and 8 other tissues.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005178; F:integrin binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:InterPro.
DR CDD; cd06263; MAM; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; IPR032930; Egfl6.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000998; MAM_dom.
DR PANTHER; PTHR24050:SF24; PTHR24050:SF24; 1.
DR Pfam; PF07645; EGF_CA; 3.
DR Pfam; PF00629; MAM; 1.
DR PRINTS; PR00020; MAMDOMAIN.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00137; MAM; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS50060; MAM_2; 1.
PE 2: Evidence at transcript level;
KW Basement membrane; Calcium; Cell adhesion; Coiled coil;
KW Developmental protein; Differentiation; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..544
FT /note="Epidermal growth factor-like protein 6"
FT /id="PRO_0000295813"
FT DOMAIN 63..98
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 100..139
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 144..178
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 180..218
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 225..265
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 399..543
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT REGION 332..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 333..367
FT /evidence="ECO:0000255"
FT DISULFID 67..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 71..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 88..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 104..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 111..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 126..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 184..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 191..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 229..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 236..251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 253..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 544 AA; 61048 MW; 24865A62D2EAB7B5 CRC64;
MAITGGMQSS DMVLLLWITV ICACCSFVDS SRSHRQLITS PSTTGVCRYG IKAECCYGWK
RNRKGQCEAV CEQGCKHGEC VGPNKCKCFP GFTGKNCNQD LNECGLKPRP CEHRCMNTHG
SYKCYCLNGY MLMPDGSCSN SRTCAMANCQ YGCEQVKGDI RCLCPSGGLQ LGPDGRTCID
IDECAVGKAS CPINRRCVNT FGSYYCKCQI GYELKYVNGR YDCIDINECL LNTHKCSINA
DCLNTQGSFK CRCKHGFKGN GQECSAVFNK PVKESPKFGG SVKDAIKKLL AHKNSLNRYN
DIKNVIPETF ITPPPKNRLQ PFDYEDGVYI GGNDNDEEEG EIEEEEEEEL DEEDEENVIE
EEKLLRGDVF ARQVKRAAVL SSQPISNTDP VLKSDEVLVD CRFDQGTCEW KQDSKDDFDW
KHAERHNGNG YYMSVPASTS QKKGIGRLKL QLTKIYYKYC LMFIYRLAGE RVGKLRVYID
ENINPIWEET KNRDEGWRTA KIEIQESSTR KSSSITFEAV RGKDEAGIMA LDNVFLSSGP
CSDD
