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Database: UniProt
Entry: H0W6T2_CAVPO
LinkDB: H0W6T2_CAVPO
Original site: H0W6T2_CAVPO 
ID   H0W6T2_CAVPO            Unreviewed;       430 AA.
AC   H0W6T2;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   31-JUL-2019, entry version 44.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCPOP00000018686};
GN   Name=Grwd1 {ECO:0000313|Ensembl:ENSCPOP00000018686};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricomorpha; Caviidae; Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000018686};
RN   [1] {ECO:0000313|Ensembl:ENSCPOP00000018686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000018686};
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:ENSCPOP00000018686}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000018686};
RG   Ensembl;
RL   Submitted (JAN-2012) 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; AAKN02046424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSCPOT00000002324; ENSCPOP00000018686; ENSCPOG00000026778.
DR   GeneTree; ENSGT00960000186595; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000002292; Expressed in 1 organ(s), highest expression level in brain.
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:UP000005447};
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:UP000005447};
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     80    106       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    118    136       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    156    180       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       47    185       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      192    363       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      394    430       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        171    171       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;  47303 MW;  7403C0F3976D1DE6 CRC64;
     MGLAKALRRL SGALDRPDDE EAAGPGLCRN GWAPAQGPGA RRRGRFVKKD GHCNVRFVNL
     GGQGARYLSD LFTTCVDVRW RWMCLLFSCS FLASWLLFGL AFWLIASLHG DLAAPPPPAP
     CFSHVASFLA AFLFALETQT SIGYGVRSVT EECPAAVAAV VLQCIAGCVL DAFVVGAVMA
     KMAKPKKRNE TLVFSENAVV ALRDRRLCLM WRVGNLRRSH LVEAHVRAQL LQPRVTPEGE
     YIPLDHQDVD VGFDGGTDRI FLVSPITIVH EIDSASPLYE LGRAELARAD FELVVILEGM
     VEATAMTTQC RSSYLPGELL WGHRFEPVLF QRGSQYEVDY RHFHRTYEVP GTPVCSAKEL
     DERAEQNAHS PKSSFPGSLA AFCYENELAL SCCQEEDEEE ETKEETGAET EDGAASPRVI
     TPTLALSLLP
//
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