EGFL6_MOUSE
ID EGFL6_MOUSE Reviewed; 550 AA.
AC Q9JJZ5; Q8BPM8;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Epidermal growth factor-like protein 6;
DE Short=EGF-like protein 6;
DE AltName: Full=MAM and EGF domains-containing gene protein;
DE AltName: Full=Protein W80;
DE Flags: Precursor;
GN Name=Egfl6; Synonyms=Maeg;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=10777661; DOI=10.1006/geno.2000.6146;
RA Buchner G., Orfanelli U., Quaderi N., Bassi M.T., Andolfi G.;
RT "Identification of a new EGF-repeat-containing gene from human Xp22: a
RT candidate for developmental disorders.";
RL Genomics 65:16-23(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-327.
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=11044626; DOI=10.1016/s0925-4773(00)00462-7;
RA Buchner G., Broccoli V., Bulfone A., Orfanelli U., Gattuso C., Ballabio A.,
RA Franco B.;
RT "MAEG, an EGF-repeat containing gene, is a new marker associated with
RT dermatome specification and morphogenesis of its derivatives.";
RL Mech. Dev. 98:179-182(2000).
RN [6]
RP FUNCTION, MUTAGENESIS OF ASP-362, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15572035; DOI=10.1016/j.yexcr.2004.04.053;
RA Osada A., Kiyozumi D., Tsutsui K., Ono Y., Weber C.N., Sugimoto N.,
RA Imai T., Okada A., Sekiguchi K.;
RT "Expression of MAEG, a novel basement membrane protein, in mouse hair
RT follicle morphogenesis.";
RL Exp. Cell Res. 303:148-159(2005).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=18757743; DOI=10.1073/pnas.0803640105;
RA Manabe R., Tsutsui K., Yamada T., Kimura M., Nakano I., Shimono C.,
RA Sanzen N., Furutani Y., Fukuda T., Oguri Y., Shimamoto K., Kiyozumi D.,
RA Sato Y., Sado Y., Senoo H., Yamashina S., Fukuda S., Kawai J., Sugiura N.,
RA Kimata K., Hayashizaki Y., Sekiguchi K.;
RT "Transcriptome-based systematic identification of extracellular matrix
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12849-12854(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May bind integrin alpha-8/beta-1 and play a role in hair
CC follicle morphogenesis. Promotes matrix assembly.
CC {ECO:0000269|PubMed:15572035, ECO:0000269|PubMed:18757743}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000269|PubMed:18757743}.
CC -!- TISSUE SPECIFICITY: Expressed at basement membrane of pelage follicles
CC (at protein level). {ECO:0000269|PubMed:15572035}.
CC -!- DEVELOPMENTAL STAGE: Detected in early lateral dermatome and in all
CC dermatome derivatives. Expressed at the basement membrane of embryonic
CC skin and developing hair follicles. At 16.5 dpc, present in lung
CC epithelium, and developing oral and tooth germ epithelia (at protein
CC level). {ECO:0000269|PubMed:11044626, ECO:0000269|PubMed:15572035,
CC ECO:0000269|PubMed:18757743}.
CC -!- SIMILARITY: Belongs to the nephronectin family. {ECO:0000305}.
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DR EMBL; AJ245672; CAB92138.1; -; mRNA.
DR EMBL; AL672174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117702; AAI17703.1; -; mRNA.
DR EMBL; AK053738; BAC35499.1; -; mRNA.
DR CCDS; CCDS30528.1; -.
DR RefSeq; NP_062270.1; NM_019397.3.
DR AlphaFoldDB; Q9JJZ5; -.
DR SMR; Q9JJZ5; -.
DR STRING; 10090.ENSMUSP00000000412; -.
DR GlyGen; Q9JJZ5; 1 site.
DR iPTMnet; Q9JJZ5; -.
DR PhosphoSitePlus; Q9JJZ5; -.
DR PaxDb; Q9JJZ5; -.
DR PRIDE; Q9JJZ5; -.
DR ProteomicsDB; 277558; -.
DR Antibodypedia; 641; 102 antibodies from 15 providers.
DR DNASU; 54156; -.
DR Ensembl; ENSMUST00000000412; ENSMUSP00000000412; ENSMUSG00000000402.
DR GeneID; 54156; -.
DR KEGG; mmu:54156; -.
DR UCSC; uc009uww.1; mouse.
DR CTD; 25975; -.
DR MGI; MGI:1858599; Egfl6.
DR VEuPathDB; HostDB:ENSMUSG00000000402; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00930000150973; -.
DR HOGENOM; CLU_036867_0_0_1; -.
DR InParanoid; Q9JJZ5; -.
DR OMA; AVCPYNR; -.
DR OrthoDB; 766075at2759; -.
DR PhylomeDB; Q9JJZ5; -.
DR TreeFam; TF330819; -.
DR BioGRID-ORCS; 54156; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Egfl6; mouse.
DR PRO; PR:Q9JJZ5; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9JJZ5; protein.
DR Bgee; ENSMUSG00000000402; Expressed in humerus cartilage element and 160 other tissues.
DR Genevisible; Q9JJZ5; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
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:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
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; IPR024731; EGF_dom.
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; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF00629; MAM; 1.
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; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS50060; MAM_2; 1.
PE 1: Evidence at protein level;
KW Basement membrane; Calcium; Cell adhesion; Coiled coil;
KW Developmental protein; Differentiation; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..550
FT /note="Epidermal growth factor-like protein 6"
FT /id="PRO_0000295812"
FT DOMAIN 55..90
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 92..131
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 135..171
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 172..210
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 217..257
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 397..543
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT REGION 295..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 327..357
FT /evidence="ECO:0000255"
FT COMPBIAS 321..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 63..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 80..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 96..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 103..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 118..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 176..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 183..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 221..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 228..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 245..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MUTAGEN 362
FT /note="D->E: Loss of adhesive activity."
FT /evidence="ECO:0000269|PubMed:15572035"
SQ SEQUENCE 550 AA; 61520 MW; DEF936325C9F31B3 CRC64;
MQPPWGLALP LLLPWVTGGV GTSPWDYGLS ALAHQPGVCQ YGTKMACCYG WKRNNKGVCE
AMCEPRCKFG ECVGPNKCRC FPGYTGKTCT QDVNECGVKP RPCQHRCVNT HGSYKCFCLS
GHMLLPDATC SNSRTCARLN CQYGCEDTEE GPRCVCPSSG LRLGPNGRVC LDIDECASSK
AVCPSNRRCV NTFGSYYCKC HIGFELKYIG RRYDCVDINE CALNTHPCSP HANCLNTRGS
FKCKCKQGYR GNGLQCSVIP EHSVKEILTA PGTIKDRIKK LLAHKRTMKK KVKLKMVTPR
PASTRVPKVN LPYSSEEGVS RGRNYDGEQK KKEEGKRERL EEEKGEKTLR NEVEQERTLR
GDVFSPKVNE AEDLDLVYVQ RKELNSKLKH KDLNISVDCS FDLGVCDWKQ DREDDFDWHP
ADRDNDVGYY MAVPALAGHK KNIGRLKLLL PNLTPQSNFC LLFDYRLAGD KVGKLRVFVK
NSNNALAWEE TKNEDGRWRT GKIQLYQGID TTKSVIFEAE RGKGKTGEIA VDGVLLVSGL
CPDDFLSVEG
