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Database: UniProt
Entry: G1PQZ8_MYOLU
LinkDB: G1PQZ8_MYOLU
Original site: G1PQZ8_MYOLU 
ID   G1PQZ8_MYOLU            Unreviewed;       431 AA.
AC   G1PQZ8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   16-OCT-2019, entry version 48.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000013536};
GN   Name=LOC102423280 {ECO:0000313|Ensembl:ENSMLUP00000013536};
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:ENSMLUP00000013536, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000013536, 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:ENSMLUP00000013536}
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; AAPE02064172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006108884.1; XM_006108822.2.
DR   STRING; 59463.ENSMLUP00000013536; -.
DR   Ensembl; ENSMLUT00000014871; ENSMLUP00000013536; ENSMLUG00000014869.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00960000186595; -.
DR   InParanoid; G1PQZ8; -.
DR   OMA; QHGSQYE; -.
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    184       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       51    189       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      196    367       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      398    431       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        175    175       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   431 AA;  47182 MW;  3B39C6A2D13F2BAF CRC64;
     MGLAEALRRL SGALESGSGG AGDEEAGPGL CRNGWAPAQS PPAGRRGGRF VKKDGHCNVR
     FVNLGGQGAR YLSDLFTTCV DVRWRWMCLL FSCSFLASWL LFGLAFWLIA SLHGDLAAPP
     PPAPCFSHVA SFLAAFLFAL ETQTSIGYGV RSVTEECPAA VAAVVLQCIA GCVLDAFVVG
     AVMAKMAKPK KRNETLIFSE NAVVALRDRR LCLMWRVGNL RRSHLVEAHV RAQLLQPRVT
     PEGEYIPLDH RDVDVGFDGG TDRIFLVSPI TIVHEIDSSS PLYELGRAEL ARADFELVVI
     LEGMVEATAM TTQCRSSYLP GELLWGHRFE PVLFQRGSQY EVDYRHFHRT YEVPGTPVCS
     AKELDERAER DSHSPKSSFP DSLTAFCYEN ELALSCCREE EEAKEGDESE AEEGAASPRG
     LTPTLSLTLP P
//
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