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Database: UniProt
Entry: A0A091KUZ0_9GRUI
LinkDB: A0A091KUZ0_9GRUI
Original site: A0A091KUZ0_9GRUI 
ID   A0A091KUZ0_9GRUI        Unreviewed;       361 AA.
AC   A0A091KUZ0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   31-JUL-2019, entry version 24.
DE   SubName: Full=Inward rectifier potassium channel 13 {ECO:0000313|EMBL:KFP44444.1};
DE   Flags: Fragment;
GN   ORFNames=N324_11822 {ECO:0000313|EMBL:KFP44444.1};
OS   Chlamydotis macqueenii (Macqueen's bustard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX   NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP44444.1};
RN   [1] {ECO:0000313|EMBL:KFP44444.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP44444.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KK759513; KFP44444.1; -; Genomic_DNA.
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; IPR008062; KCNJ13.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF3; PTHR11767:SF3; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01679; KIR7CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Ion channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434609, ECO:0000313|EMBL:KFP44444.1};
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   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     56     79       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    135    159       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       21    164       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      171    325       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      325    347       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    332    346       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        150    150       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium.
FT                                {ECO:0000256|PIRSR:PIRSR005465-1}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:KFP44444.1}.
FT   NON_TER     361    361       {ECO:0000313|EMBL:KFP44444.1}.
SQ   SEQUENCE   361 AA;  40671 MW;  9CAAD7C4DB9B0096 CRC64;
     LESNNTKSSA PLLTQRYLRM VTKDGHSTFQ MNGAQGKGLA YLRDAWGILM DMRWRWMMLV
     FSASFVIHWL VFAVLWYLLA EMNGDLELDH DAPPDNHTIC VKYITSFTAA FSFSLETQLT
     IGYGTMFPSG DCPSAIALLA IQMVLGLMLE AFITGAFVAK IARPKNRAFS IRFTRSAIVT
     HTEGKPCLMF QVANTRSSPL TSVQISAILY QEQENGQLHQ TSVDFHLDSI TLDECPFFIF
     PLTYYHSITP SSPLALLLQR EATHHFELVV FLSAVQEGTG ETCQRRTSYL PSEIMLYHRF
     ASVLARNAKG EYQIKMENFD KTIPELPATA DSKSPKRTDK EIRINGQHAD SFQLSETGLI
     E
//
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