ID MEGF9_MOUSE Reviewed; 600 AA.
AC Q8BH27; Q8BWI4;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 148.
DE RecName: Full=Multiple epidermal growth factor-like domains protein 9;
DE Short=Multiple EGF-like domains protein 9;
DE AltName: Full=Epidermal growth factor-like protein 5;
DE Short=EGF-like protein 5;
DE Flags: Precursor;
GN Name=Megf9; Synonyms=Egfl5, Kiaa0818;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Lung, and Spinal cord;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AK035987; BAC29269.1; -; mRNA.
DR EMBL; AK039319; BAC30317.1; -; mRNA.
DR EMBL; AK052434; BAC34987.1; -; mRNA.
DR EMBL; AK122378; BAC65660.1; -; mRNA.
DR CCDS; CCDS18273.1; -.
DR RefSeq; NP_766282.1; NM_172694.2.
DR AlphaFoldDB; Q8BH27; -.
DR SMR; Q8BH27; -.
DR STRING; 10090.ENSMUSP00000102982; -.
DR GlyConnect; 2517; 2 N-Linked glycans (2 sites).
DR GlyCosmos; Q8BH27; 12 sites, 2 glycans.
DR GlyGen; Q8BH27; 12 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; Q8BH27; -.
DR PhosphoSitePlus; Q8BH27; -.
DR CPTAC; non-CPTAC-4046; -.
DR PaxDb; 10090-ENSMUSP00000102982; -.
DR ProteomicsDB; 292192; -.
DR Antibodypedia; 2992; 180 antibodies from 23 providers.
DR DNASU; 230316; -.
DR Ensembl; ENSMUST00000107359.9; ENSMUSP00000102982.3; ENSMUSG00000039270.10.
DR GeneID; 230316; -.
DR KEGG; mmu:230316; -.
DR UCSC; uc008tib.1; mouse.
DR AGR; MGI:1918264; -.
DR CTD; 1955; -.
DR MGI; MGI:1918264; Megf9.
DR VEuPathDB; HostDB:ENSMUSG00000039270; -.
DR eggNOG; KOG0994; Eukaryota.
DR GeneTree; ENSGT00940000161177; -.
DR HOGENOM; CLU_031674_2_0_1; -.
DR InParanoid; Q8BH27; -.
DR OMA; YIGPNCN; -.
DR OrthoDB; 5491831at2759; -.
DR PhylomeDB; Q8BH27; -.
DR BioGRID-ORCS; 230316; 1 hit in 78 CRISPR screens.
DR ChiTaRS; Megf9; mouse.
DR PRO; PR:Q8BH27; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BH27; Protein.
DR Bgee; ENSMUSG00000039270; Expressed in otolith organ and 227 other cell types or tissues.
DR ExpressionAtlas; Q8BH27; baseline and differential.
DR Genevisible; Q8BH27; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 5.
DR Gene3D; 2.10.25.10; Laminin; 5.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF298; MULTIPLE EPIDERMAL GROWTH FACTOR-LIKE DOMAINS PROTEIN 9; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; Laminin_EGF; 5.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00180; EGF_Lam; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01248; EGF_LAM_1; 5.
DR PROSITE; PS50027; EGF_LAM_2; 5.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Laminin EGF-like domain; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..600
FT /note="Multiple epidermal growth factor-like domains
FT protein 9"
FT /id="PRO_0000007527"
FT TOPO_DOM 35..512
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 534..600
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 202..251
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 252..298
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 299..346
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 347..397
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 398..449
FT /note="Laminin EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 33..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 202..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 204..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 224..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 236..249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 252..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 254..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 272..281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 284..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 299..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 301..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 318..327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 330..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 347..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 349..369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 372..381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 384..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 398..413
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 400..420
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 423..432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 435..447
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 600 AA; 62831 MW; 556381D182971070 CRC64;
MNGGAERAMR SLPSLGGLAL LCCAAAAAAS TASAGNVTGG GGAEGQVVPS PSPGLRDQAS
SPFPKTAAPT AQAPRTGPPR TTVRKTGATT PSAGSPEIIP PLRTSAQPAA TPFPALDLSP
ATPSEDGHTP TTESPPSRPA PTTLASTVGQ PPTTSVVTTA QASSTPGTPT AESPDRSSNS
SGVPPTAPVT EAPTSPPPEH MCNCSEVGSL DVKRCNQTTG QCDCHVGYQG LHCDTCKEGF
YLNHTVGLCL PCHCSPHGAV SILCNSSGNC QCKVGVTGSM CDKCQDGHYG FGKTGCLPCQ
CNNRSDSCDV HTGACLNCQE NSKGEHCEEC KEGFYPSPDA AKQCHRCPCS AVTSTGNCTI
ESGELEPTCD QCKDGYTGQN CNKCENGYYN SDSICTQCEC HGHVDPIKTP KICKPESGEC
INCLHNTTGF WCEKCLEGYV RDLQRNCIKQ EVIVPTPEGS TILVSNASLT TSVPTPVINS
TFAPTTLQTI FAVSSSENST SALADVSWTQ FNIIILTVII IVVVLLMGFV GAVYMYREYQ
NRKLNAPFWT IELKEDNISF SSYHDSIPNA DVSGLLEDDA NEVAPNGQLT LTTPIHNYKA
//
