EGFL7_RAT
ID EGFL7_RAT Reviewed; 279 AA.
AC Q6AZ60; Q9JKW3;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Epidermal growth factor-like protein 7;
DE Short=EGF-like protein 7;
DE AltName: Full=Multiple epidermal growth factor-like domains protein 7;
DE Short=Multiple EGF-like domains protein 7;
DE Flags: Precursor;
GN Name=Egfl7; Synonyms=Cbl20, Megf7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RA Chan M.T.W., Ng C.C.Y., Lim E.K.B., Huynh H.T.;
RT "Cloning and characterization of a novel 20.4kD estrogen-regulated protein
RT in the rat spleen.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Regulates vascular tubulogenesis in vivo. Inhibits platelet-
CC derived growth factor (PDGF)-BB-induced smooth muscle cell migration
CC and promotes endothelial cell adhesion to the extracellular matrix and
CC angiogenesis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ITGAV/ITGB3 in an RGD-dependent manner,
CC increasing endothelial cell's motility. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6AZ60-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6AZ60-2; Sequence=VSP_011766;
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DR EMBL; AF223678; AAF35352.1; -; mRNA.
DR EMBL; BC078725; AAH78725.1; -; mRNA.
DR RefSeq; NP_620804.1; NM_139104.1. [Q6AZ60-2]
DR AlphaFoldDB; Q6AZ60; -.
DR STRING; 10116.ENSRNOP00000026318; -.
DR PaxDb; Q6AZ60; -.
DR GeneID; 245963; -.
DR KEGG; rno:245963; -.
DR UCSC; RGD:708507; rat. [Q6AZ60-1]
DR CTD; 51162; -.
DR RGD; 708507; Egfl7.
DR VEuPathDB; HostDB:ENSRNOG00000019388; -.
DR eggNOG; KOG1217; Eukaryota.
DR HOGENOM; CLU_083642_0_0_1; -.
DR InParanoid; Q6AZ60; -.
DR OMA; CPGWRRV; -.
DR OrthoDB; 749722at2759; -.
DR PhylomeDB; Q6AZ60; -.
DR PRO; PR:Q6AZ60; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000019388; Expressed in lung and 19 other tissues.
DR Genevisible; Q6AZ60; RN.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005112; F:Notch binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0001568; P:blood vessel development; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISO:RGD.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:RGD.
DR GO; GO:0001570; P:vasculogenesis; ISS:UniProtKB.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR011489; EMI_domain.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF07546; EMI; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS51041; EMI; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Angiogenesis; Calcium; Cell adhesion; Coiled coil;
KW Developmental protein; Differentiation; Disulfide bond; EGF-like domain;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..279
FT /note="Epidermal growth factor-like protein 7"
FT /id="PRO_0000007530"
FT DOMAIN 28..109
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 108..140
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 142..182
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT COILED 200..224
FT /evidence="ECO:0000255"
FT COILED 250..274
FT /evidence="ECO:0000255"
FT MOTIF 131..133
FT /note="Cell attachment site"
FT /evidence="ECO:0000250"
FT DISULFID 32..94
FT /evidence="ECO:0000250"
FT DISULFID 57..63
FT /evidence="ECO:0000250"
FT DISULFID 93..107
FT /evidence="ECO:0000250"
FT DISULFID 112..122
FT /evidence="ECO:0000250"
FT DISULFID 116..128
FT /evidence="ECO:0000250"
FT DISULFID 130..139
FT /evidence="ECO:0000250"
FT DISULFID 146..157
FT /evidence="ECO:0000250"
FT DISULFID 153..166
FT /evidence="ECO:0000250"
FT DISULFID 168..181
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..109
FT /note="MWGSGELLVAWFLVLAAGGTTEHVYRPSRRVCTVGVSGGSISETFVQRVYQP
FT YLTTCDGHRACSTYRTIYRTAYRIAYRHSPGLTPSRPRYACCPGWKRTNGLPGACGA
FT -> MPQGSGNSPEWVTDRPLLPT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_011766"
SQ SEQUENCE 279 AA; 30371 MW; 01F2B70BDE22AD36 CRC64;
MWGSGELLVA WFLVLAAGGT TEHVYRPSRR VCTVGVSGGS ISETFVQRVY QPYLTTCDGH
RACSTYRTIY RTAYRIAYRH SPGLTPSRPR YACCPGWKRT NGLPGACGAA ICQPPCGNEG
SCIRPGRCRC PVGWQGDTCQ IDVDECSTGE ARCPQRCVNT VGSYWCQCWE GQSPSADGVL
CLPKEGPSPV APSPTPGVDS VVREEVYKLQ ARVDVLEQKL QLVLAPLHSL ASRSPEHGLQ
DPGSLLAHSF QQLDRIDSLS EQVSFLEEQL GSCSCKKDL
