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Database: UniProt
Entry: H3AKZ6_LATCH
LinkDB: H3AKZ6_LATCH
Original site: H3AKZ6_LATCH 
ID   H3AKZ6_LATCH            Unreviewed;       396 AA.
AC   H3AKZ6;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   16-OCT-2019, entry version 42.
DE   SubName: Full=Si:ch211-113j13.2 {ECO:0000313|Ensembl:ENSLACP00000010317};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000010317, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Ensembl:ENSLACP00000010317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Ensembl:ENSLACP00000010317};
RX   PubMed=9215903;
RA   Zardoya R., Meyer A.;
RT   "The complete DNA sequence of the mitochondrial genome of a 'living
RT   fossil,' the coelacanth (Latimeria chalumnae).";
RL   Genetics 146:995-1010(1997).
RN   [2] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSLACP00000010317}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-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; AFYH01099651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01099652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7897.ENSLACP00000010317; -.
DR   Ensembl; ENSLACT00000010395; ENSLACP00000010317; ENSLACG00000009087.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00970000193347; -.
DR   InParanoid; H3AKZ6; -.
DR   OMA; SHTIDEA; -.
DR   TreeFam; TF313676; -.
DR   Proteomes; UP000008672; 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:UP000008672};
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:UP000008672};
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     63     85       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    140    163       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       29    168       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      175    344       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      372    396       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        154    154       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   396 AA;  46208 MW;  1FF3535095DBD138 CRC64;
     DQNQKRCKLI DSNRQHFNVQ PTRLRQRYVT KDGKCRVNLG NIEEKGRFLS DIFTTIVDLK
     YRWFLFIFMM CYIITWVFFA SVYYLDALLR HDVYHVGDRN WQPCFQNVEN FLSALLFSVE
     TQRTIGYGTR MVTSSCPEGV YLIMAQSIVG SMIDAMMVGC MFVKISRPKK RAQTLLFSEN
     AVIANRDENL CFMFRIGDLR DSHMVDAKIR AKLIKSRQTT EGEFLPLEQS EINLGYETGE
     DRLFLVEPQV ISHTIDEASP FWELGADQLK QEQFEIIIIL EGIVEATGMT CQAKTSYIET
     EILWAHRFEP CMMLAKGEFR VDYSRFHKTF EIQMMRSSAK GNQELREMEQ EEDPSTLSLY
     WESTELHPVM ADEKEKEGEG FTEPNARSFD NIVEEQ
//
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