GenomeNet

Database: UniProt
Entry: Q9JJZ5
LinkDB: Q9JJZ5
Original site: Q9JJZ5 
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   10-APR-2019, entry version 134.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   project: 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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.,
RA   Ballabio A., 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
RP   DEVELOPMENTAL 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.,
RA   Kiyozumi D., Sato Y., Sado Y., Senoo H., Yamashina S., Fukuda S.,
RA   Kawai J., Sugiura N., 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
RT   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
CC       follicles (at protein level). {ECO:0000269|PubMed:15572035}.
CC   -!- DEVELOPMENTAL STAGE: Detected in early lateral dermatome and in
CC       all dermatome derivatives. Expressed at the basement membrane of
CC       embryonic skin and developing hair follicles. At 16.5 dpc, present
CC       in lung epithelium, and developing oral and tooth germ epithelia
CC       (at protein level). {ECO:0000269|PubMed:11044626,
CC       ECO:0000269|PubMed:15572035, ECO:0000269|PubMed:18757743}.
CC   -!- SIMILARITY: Belongs to the nephronectin family. {ECO:0000305}.
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   UniGene; Mm.37707; -.
DR   ProteinModelPortal; Q9JJZ5; -.
DR   SMR; Q9JJZ5; -.
DR   STRING; 10090.ENSMUSP00000000412; -.
DR   iPTMnet; Q9JJZ5; -.
DR   PhosphoSitePlus; Q9JJZ5; -.
DR   PaxDb; Q9JJZ5; -.
DR   PRIDE; Q9JJZ5; -.
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   eggNOG; ENOG410KD9I; Eukaryota.
DR   eggNOG; ENOG410XR84; LUCA.
DR   GeneTree; ENSGT00930000150973; -.
DR   HOGENOM; HOG000059638; -.
DR   HOVERGEN; HBG108200; -.
DR   InParanoid; Q9JJZ5; -.
DR   OMA; QYGCEDT; -.
DR   OrthoDB; 766075at2759; -.
DR   TreeFam; TF330819; -.
DR   PRO; PR:Q9JJZ5; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   Bgee; ENSMUSG00000000402; Expressed in 186 organ(s), highest expression level in embryo.
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:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion 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:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
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; IPR013032; EGF-like_CS.
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; PTHR44771; PTHR44771; 1.
DR   Pfam; PF07645; EGF_CA; 3.
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   Complete proteome; Developmental protein; Differentiation;
KW   Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19    550       Epidermal growth factor-like protein 6.
FT                                /FTId=PRO_0000295812.
FT   DOMAIN       55     90       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       92    131       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      135    171       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      172    210       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      217    257       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      397    543       MAM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00128}.
FT   COILED      327    357       {ECO:0000255}.
FT   CARBOHYD    394    394       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     59     72       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     63     78       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     80     89       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     96    107       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    103    116       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    118    130       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    176    189       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    183    198       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    221    234       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    228    243       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    245    256       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   MUTAGEN     362    362       D->E: Loss of adhesive activity.
FT                                {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
//
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