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Database: UniProt
Entry: G1QA51_MYOLU
LinkDB: G1QA51_MYOLU
Original site: G1QA51_MYOLU 
ID   G1QA51_MYOLU            Unreviewed;       746 AA.
AC   G1QA51;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   05-JUN-2019, entry version 52.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000020584};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera;
OC   Vespertilionidae; Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000020584, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000020584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Genome Sequencing Platform;
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S.,
RA   Lindblad-Toh K.;
RT   "The Genome Sequence of Myotis lucifugus (Bat).";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J.,
RA   Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E.,
RA   Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J.,
RA   Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S.,
RA   Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I.,
RA   Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I.,
RA   Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J.,
RA   Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D.,
RA   Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L.,
RA   Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S.,
RA   Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G.,
RA   Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K.,
RA   Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T.,
RA   Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J.,
RA   Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S.,
RA   Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29
RT   mammals.";
RL   Nature 478:476-482(2011).
RN   [3] {ECO:0000313|Ensembl:ENSMLUP00000020584}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2011) to UniProtKB.
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DR   EMBL; AAPE02001913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 59463.ENSMLUP00000020584; -.
DR   Ensembl; ENSMLUT00000023774; ENSMLUP00000020584; ENSMLUG00000029740.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000162672; -.
DR   InParanoid; G1QA51; -.
DR   OMA; NCWSTDY; -.
DR   TreeFam; TF314733; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001074};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068,
KW   ECO:0000256|SAAS:SAAS00877335};
KW   Membrane {ECO:0000256|SAAS:SAAS01078504, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW   Transmembrane {ECO:0000256|SAAS:SAAS01078486,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS01078482,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    689    710       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      207    387       Peptidase M12B. {ECO:0000259|PROSITE:
FT                                PS50215}.
FT   DOMAIN      408    494       Disintegrin. {ECO:0000259|PROSITE:
FT                                PS50214}.
FT   REGION      717    746       Disordered. {ECO:0000256|MobiDB-lite:
FT                                G1QA51}.
FT   DISULFID    466    486       {ECO:0000256|PROSITE-ProRule:PRU00068}.
SQ   SEQUENCE   746 AA;  84087 MW;  F4D756B148EDEEA3 CRC64;
     MAVSEALVCV RNTLLPLWLG VILFPYGWFQ VVHSQRHGPP EVVIPLKVTG TGIGMKIGDW
     LSYSLHFGGQ RHIVHMKVNR NFLSRHFRVV TYSDQGALLE ERPFIQNDCY YHGYVEGDPE
     SLVALSTCLG GLQGILQTND IVYEIEPKRR STTFEHLLYR IKSEETQLPP MKCGLTDEEI
     ARQLNFPESA NFTLMQSGYE GWWTHRGLLE LAVVVDHNRY LHHLSNTTAV QYEVLLVVNG
     VAKFLSSLDV DVVLMGIEVW TEKNPVPIDT IDGLLEEFCK WKKTSLNNRI PNDVAHLFVK
     HSYGTTAGLA YIKTICKSYA SCGVDSFMND NVYDFAYIVS HEIGHNLGMD HDGPTCTCGH
     KTCIMFPENE SATRFSNCSY ADFMDMMGTI ARKNCLYISS NTGNIFTLAR CGNSVIEEGE
     ECDCGTLHLC MKDPCCESNC TLSPGAACAF GLCCKDCQIL PTGEVCRQEE NECDLPEWCN
     GTSYHCPEDV YLQNGMPCKG GGSCYEKRCN NREEQCRNIF GKEAKSANQS CYTEINTQGD
     RFGNCGFKHS RYVKCDISDT LCGRIQCDNV TELPLLRNHS TVHWTQFNGA TCWGTDYHFG
     LTEPDIGDVK DGTECGAEHV CIQRKCVHRS LLVNYCSPEM CNLKGVCNNR HHCHCNYDWD
     PPKCIKEGSG GSIDSGPPPR KKIRKKTQYL QLLWLLPFIL LLCLLVLCFL TRRRKDKSEE
     QSVSLSAEKE EQNVKTLPRE NEQDVA
//
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