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Database: UniProt
Entry: G1Q560_MYOLU
LinkDB: G1Q560_MYOLU
Original site: G1Q560_MYOLU 
ID   G1Q560_MYOLU            Unreviewed;       430 AA.
AC   G1Q560;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   16-OCT-2019, entry version 43.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000018843};
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:ENSMLUP00000018843, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000018843, 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   [2] {ECO:0000313|Ensembl:ENSMLUP00000018843}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2011) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003822};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU003822}.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC       (TC 1.A.2.1) family. {ECO:0000256|RuleBase:RU003822,
CC       ECO:0000256|SAAS:SAAS00549381}.
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DR   EMBL; AAPE02064466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 59463.ENSMLUP00000018843; -.
DR   Ensembl; ENSMLUT00000023886; ENSMLUP00000018843; ENSMLUG00000028888.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00960000186595; -.
DR   InParanoid; G1Q560; -.
DR   OMA; LSCCHEE; -.
DR   TreeFam; TF313676; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IEA:InterPro.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1400; -; 1.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR041647; IRK_C.
DR   InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001074};
KW   Ion channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434609};
KW   Ion transport {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434639};
KW   Membrane {ECO:0000256|SAAS:SAAS00434581, ECO:0000256|SAM:Phobius};
KW   Potassium {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434575};
KW   Potassium transport {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434641};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW   Transmembrane {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434543, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00036756,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00036755};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00048561}.
FT   TRANSMEM     84    110       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    122    140       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    160    183       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       51    188       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      195    366       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      397    430       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        174    174       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium.
FT                                {ECO:0000256|PIRSR:PIRSR005465-1}.
SQ   SEQUENCE   430 AA;  47270 MW;  B2D98CFDB6DDE666 CRC64;
     MGLAEALRRL SGTLESGSGG AGDEEAGLGL CRNGWAPAQS PPAGRRGGRF VKKDGHCNVR
     FVNLGGQGAR YLSDLFTTCV DVRWRWMCLL FSCSFLASWL LFGLAFWLIA SLHGDLAAPP
     PPAPCFSHVA SFLAAFLFAL ETQTSIGYGV RSVTEECPAA VAAVVLQCIG CVLDAFVVGA
     VMAKMAKPKK RNETLIFSEN AVVALRDRRL CLMWRVRNLR RSHLVEAHVR VQLLQPRVTP
     EGEYIPLDHR DVDVGFDGGT DRIFLVSPIT IVHEIDSSSP LYELGRAELA RADFELVVIL
     EGMVEATAMT TQCRSSYLPG ELLWGHRFEP VLFQRGSQYE VDYRHFHRTY EVPGTPVCSA
     KELDERAERD SHSPKSSFPD SLTAFCYENE LALSCCREEE EAKEGDESEA EEGAGSPRGL
     TPTLSLTLPP
//
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