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Database: UniProt
Entry: A0A091MC14_CARIC
LinkDB: A0A091MC14_CARIC
Original site: A0A091MC14_CARIC 
ID   A0A091MC14_CARIC        Unreviewed;       361 AA.
AC   A0A091MC14;
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:KFP69056.1};
DE   Flags: Fragment;
GN   ORFNames=N322_01597 {ECO:0000313|EMBL:KFP69056.1};
OS   Cariama cristata (Red-legged seriema).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cariamiformes; Cariamidae; Cariama.
OX   NCBI_TaxID=54380 {ECO:0000313|EMBL:KFP69056.1};
RN   [1] {ECO:0000313|EMBL:KFP69056.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N322 {ECO:0000313|EMBL:KFP69056.1};
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; KK528645; KFP69056.1; -; 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:KFP69056.1};
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    361       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:KFP69056.1}.
FT   NON_TER     361    361       {ECO:0000313|EMBL:KFP69056.1}.
SQ   SEQUENCE   361 AA;  40634 MW;  05EF60CEF99399A0 CRC64;
     IESNNIKSSA PLLTQRYLRM VTKDGHSTFQ MDGTQGKGLA YLRDAWGILM DMRWRWMMLV
     FSASFVIHWL VFAVLWYLLA EMNGDLELDH DAPPDNHTIC VKYITSFTAA FSFSLETQLT
     IGYGTMFPSG DCPSAIALLA IQMVLGLMLE AFITGAFVAK IARPKNRAFS IRFTHSAVVT
     YTDGKPYLKF QVANTRSSPL TSVQISAILY QEQENGQLHQ TSVDFHLDSV TSDECPFFIF
     PLTYYHSITP SSPLAALLQR EAAHHFELVI FLSAVQEGTG ETCQRRTSYL PSEIMLYHRF
     ASVLARNAKG EYRIKMENFD KTIPELPATA DSKSPKRTDK EIRINGQHAD SLQLSETGLT
     E
//
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