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Database: UniProt
Entry: Q9UHF1
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ID   EGFL7_HUMAN             Reviewed;         273 AA.
AC   Q9UHF1; B3KRP0; M9VTX9; Q5M7Y5; Q5VUD5; Q96EG0;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 3.
DT   10-APR-2019, entry version 152.
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   AltName: Full=NOTCH4-like protein;
DE   AltName: Full=Vascular endothelial statin;
DE            Short=VE-statin;
DE   AltName: Full=Zneu1;
DE   Flags: Precursor;
GN   Name=EGFL7; Synonyms=MEGF7; ORFNames=UNQ187/PRO1449;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Sheppard P., Jelinek L., Whitmore T., Blumberg H., Lehner J.,
RA   O'Hara P.;
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-153.
RA   Tanaka S., Maehara M.;
RT   "A novel gene regulating tumor angiogenesis.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-114.
RA   Hong S.M., Sung H.S.;
RT   "Characterization of recombinant human epidermal growth factor like-7
RT   (rhEGFL7) produced by Bombyx mori.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-153.
RC   TISSUE=Kidney;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-153.
RC   TISSUE=Brain, and Ovary;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, CELL ATTACHMENT MOTIF, AND
RP   MUTAGENESIS OF GLY-131.
RX   PubMed=23386126; DOI=10.1182/blood-2011-11-394882;
RA   Nikolic I., Stankovic N.D., Bicker F., Meister J., Braun H., Awwad K.,
RA   Baumgart J., Simon K., Thal S.C., Patra C., Harter P.N., Plate K.H.,
RA   Engel F.B., Dimmeler S., Eble J.A., Mittelbronn M., Schafer M.K.,
RA   Jungblut B., Chavakis E., Fleming I., Schmidt M.H.;
RT   "EGFL7 ligates alphavbeta3 integrin to enhance vessel formation.";
RL   Blood 121:3041-3050(2013).
RN   [10]
RP   FUNCTION, AND MISCELLANEOUS.
RX   PubMed=23639441; DOI=10.1016/j.devcel.2013.03.003;
RA   Charpentier M.S., Christine K.S., Amin N.M., Dorr K.M., Kushner E.J.,
RA   Bautch V.L., Taylor J.M., Conlon F.L.;
RT   "CASZ1 promotes vascular assembly and morphogenesis through the direct
RT   regulation of an EGFL7/RhoA-mediated pathway.";
RL   Dev. Cell 25:132-143(2013).
CC   -!- FUNCTION: Regulates vascular tubulogenesis in vivo. Inhibits
CC       platelet-derived growth factor (PDGF)-BB-induced smooth muscle
CC       cell migration and promotes endothelial cell adhesion to the
CC       extracellular matrix and angiogenesis.
CC       {ECO:0000269|PubMed:23386126, ECO:0000269|PubMed:23639441}.
CC   -!- SUBUNIT: Interacts with ITGAV/ITGB3 in an RGD-dependent manner,
CC       increasing endothelial cell's motility.
CC       {ECO:0000269|PubMed:23386126}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|PubMed:23386126}.
CC   -!- MISCELLANEOUS: Endothelial cells depleted in EGFL7 by siRNAs
CC       display dramatic alterations in adhesion, morphology, and
CC       sprouting. The defects are in part due to diminished RhoA
CC       expression and impaired focal adhesion localization.
DR   EMBL; AF186111; AAF01429.1; -; mRNA.
DR   EMBL; AB125649; BAD01469.1; -; mRNA.
DR   EMBL; KC485578; AGJ83826.1; -; mRNA.
DR   EMBL; AL512735; CAC21666.1; -; mRNA.
DR   EMBL; AY358901; AAQ89260.1; -; mRNA.
DR   EMBL; AY358902; AAQ89261.1; -; mRNA.
DR   EMBL; AY358903; AAQ89262.1; -; mRNA.
DR   EMBL; AK091964; BAG52452.1; -; mRNA.
DR   EMBL; AL590226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC012377; AAH12377.1; -; mRNA.
DR   EMBL; BC088371; AAH88371.1; -; mRNA.
DR   CCDS; CCDS7002.1; -.
DR   RefSeq; NP_057299.1; NM_016215.4.
DR   RefSeq; NP_958854.1; NM_201446.2.
DR   RefSeq; XP_011517066.1; XM_011518764.1.
DR   RefSeq; XP_011517067.1; XM_011518765.1.
DR   RefSeq; XP_011517068.1; XM_011518766.1.
DR   UniGene; Hs.91481; -.
DR   ProteinModelPortal; Q9UHF1; -.
DR   SMR; Q9UHF1; -.
DR   BioGrid; 119343; 46.
DR   IntAct; Q9UHF1; 22.
DR   MINT; Q9UHF1; -.
DR   STRING; 9606.ENSP00000360764; -.
DR   ChEMBL; CHEMBL3712972; -.
DR   iPTMnet; Q9UHF1; -.
DR   PhosphoSitePlus; Q9UHF1; -.
DR   BioMuta; EGFL7; -.
DR   DMDM; 92090985; -.
DR   EPD; Q9UHF1; -.
DR   jPOST; Q9UHF1; -.
DR   MaxQB; Q9UHF1; -.
DR   PaxDb; Q9UHF1; -.
DR   PeptideAtlas; Q9UHF1; -.
DR   PRIDE; Q9UHF1; -.
DR   ProteomicsDB; 84339; -.
DR   DNASU; 51162; -.
DR   Ensembl; ENST00000308874; ENSP00000307843; ENSG00000172889.
DR   Ensembl; ENST00000371698; ENSP00000360763; ENSG00000172889.
DR   Ensembl; ENST00000371699; ENSP00000360764; ENSG00000172889.
DR   Ensembl; ENST00000406555; ENSP00000385639; ENSG00000172889.
DR   GeneID; 51162; -.
DR   KEGG; hsa:51162; -.
DR   UCSC; uc004cid.3; human.
DR   CTD; 51162; -.
DR   DisGeNET; 51162; -.
DR   EuPathDB; HostDB:ENSG00000172889.15; -.
DR   GeneCards; EGFL7; -.
DR   H-InvDB; HIX0058702; -.
DR   HGNC; HGNC:20594; EGFL7.
DR   HPA; HPA050716; -.
DR   MIM; 608582; gene.
DR   neXtProt; NX_Q9UHF1; -.
DR   OpenTargets; ENSG00000172889; -.
DR   PharmGKB; PA134928613; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; ENOG410XP6K; LUCA.
DR   GeneTree; ENSGT00940000160015; -.
DR   HOGENOM; HOG000231494; -.
DR   HOVERGEN; HBG051453; -.
DR   InParanoid; Q9UHF1; -.
DR   OMA; PQHCVNT; -.
DR   OrthoDB; 749722at2759; -.
DR   PhylomeDB; Q9UHF1; -.
DR   TreeFam; TF331360; -.
DR   GeneWiki; EGFL7; -.
DR   GenomeRNAi; 51162; -.
DR   PRO; PR:Q9UHF1; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   Bgee; ENSG00000172889; Expressed in 203 organ(s), highest expression level in right lung.
DR   ExpressionAtlas; Q9UHF1; baseline and differential.
DR   Genevisible; Q9UHF1; HS.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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:0045746; P:negative regulation of Notch signaling pathway; IMP:MGI.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:MGI.
DR   GO; GO:0001570; P:vasculogenesis; ISS:UniProtKB.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR011489; EMI_domain.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
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   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS51041; EMI; 1.
PE   1: Evidence at protein level;
KW   Angiogenesis; Calcium; Cell adhesion; Coiled coil; Complete proteome;
KW   Developmental protein; Differentiation; Disulfide bond;
KW   EGF-like domain; Polymorphism; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    273       Epidermal growth factor-like protein 7.
FT                                /FTId=PRO_0000007528.
FT   DOMAIN       27    104       EMI. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00384}.
FT   DOMAIN      103    135       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      137    177       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   COILED      192    219       {ECO:0000255}.
FT   MOTIF       130    132       Cell attachment site.
FT   DISULFID     31     89       {ECO:0000250}.
FT   DISULFID     56     62       {ECO:0000250}.
FT   DISULFID     88    102       {ECO:0000250}.
FT   DISULFID    107    117       {ECO:0000250}.
FT   DISULFID    111    123       {ECO:0000250}.
FT   DISULFID    125    134       {ECO:0000250}.
FT   DISULFID    141    152       {ECO:0000250}.
FT   DISULFID    148    161       {ECO:0000250}.
FT   DISULFID    163    176       {ECO:0000250}.
FT   VARIANT     114    114       G -> R (in dbSNP:rs61736886).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_070951.
FT   VARIANT     153    153       V -> I (in dbSNP:rs2297538).
FT                                {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019791.
FT   VARIANT     183    183       P -> S (in dbSNP:rs35863900).
FT                                /FTId=VAR_048981.
FT   VARIANT     186    186       A -> G (in dbSNP:rs34142075).
FT                                /FTId=VAR_048982.
FT   MUTAGEN     131    131       G->A: Disrupts RGD motif and results in a
FT                                79% loss of cell adhesion.
FT                                {ECO:0000269|PubMed:23386126}.
SQ   SEQUENCE   273 AA;  29618 MW;  5740BB845ED5A988 CRC64;
     MRGSQEVLLM WLLVLAVGGT EHAYRPGRRV CAVRAHGDPV SESFVQRVYQ PFLTTCDGHR
     ACSTYRTIYR TAYRRSPGLA PARPRYACCP GWKRTSGLPG ACGAAICQPP CRNGGSCVQP
     GRCRCPAGWR GDTCQSDVDE CSARRGGCPQ RCVNTAGSYW CQCWEGHSLS ADGTLCVPKG
     GPPRVAPNPT GVDSAMKEEV QRLQSRVDLL EEKLQLVLAP LHSLASQALE HGLPDPGSLL
     VHSFQQLGRI DSLSEQISFL EEQLGSCSCK KDS
//
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