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Database: UniProt
Entry: A0A2G9QI38_LITCT
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ID   A0A2G9QI38_LITCT        Unreviewed;       409 AA.
AC   A0A2G9QI38;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   11-DEC-2019, entry version 12.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PIO15227.1};
GN   ORFNames=AB205_0008930 {ECO:0000313|EMBL:PIO15227.1};
OS   Lithobates catesbeiana (American bullfrog) (Rana catesbeiana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Aquarana.
OX   NCBI_TaxID=8400 {ECO:0000313|EMBL:PIO15227.1, ECO:0000313|Proteomes:UP000228934};
RN   [1] {ECO:0000313|Proteomes:UP000228934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=29127278; DOI=10.1038/s41467-017-01316-7;
RA   Hammond S.A., Warren R.L., Vandervalk B.P., Kucuk E., Khan H., Gibb E.A.,
RA   Pandoh P., Kirk H., Zhao Y., Jones M., Mungall A.J., Coope R.,
RA   Pleasance S., Moore R.A., Holt R.A., Round J.M., Ohora S., Walle B.V.,
RA   Veldhoen N., Helbing C.C., Birol I.;
RT   "The North American bullfrog draft genome provides insight into hormonal
RT   regulation of long noncoding RNA.";
RL   Nat. Commun. 8:1433-1433(2017).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003822}; Multi-
CC       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; KV982141; PIO15227.1; -; Genomic_DNA.
DR   Proteomes; UP000228934; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015467; F:G-protein activated 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; IPR003276; K_chnl_inward-rec_Kir3.3.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF17; PTHR11767:SF17; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01329; KIR33CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Ion channel {ECO:0000256|RuleBase:RU003822, 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, 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, ECO:0000256|SAAS:SAAS00036755};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00048561}.
FT   TRANSMEM        82..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          46..185
FT                   /note="IRK"
FT                   /evidence="ECO:0000259|Pfam:PF01007"
FT   DOMAIN          192..362
FT                   /note="IRK_C"
FT                   /evidence="ECO:0000259|Pfam:PF17655"
FT   REGION          379..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..409
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            171
FT                   /note="Role in the control of polyamine-mediated channel
FT                   gating and in the blocking by intracellular magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005465-1"
SQ   SEQUENCE   409 AA;  46695 MW;  BAE6F5916CC73C10 CRC64;
     MAKDNNVFTP IPGPTITNTK AFTHAAKLAE KLEKADRKLR RRQRYVEKDG RCNVQHGNVR
     ETYRYLTDIF TTLVDLKWRV SLLVFIMAYA ITWLFFGVIW WFIAYCRGDL EHLEDPGWTP
     CIKNLNGFVS AFLFSIETET TIGYGHRVIT DKCPEGIILL LLQAILGSMV NAFMVGCMFV
     KISQPNKRAE TLVFSSHAVI SLRDDKLCLM FRVGDLRQSH IVEASIRAKL IKSKQTQEGE
     FIPLNQTDIN VGFETGDDRL FLVSPLIISH EINEHSPFWE VSKRQLAMDD FEIVVILEGM
     VEATGMTCQA RSSYLVDEVQ WGHRFMSVLS LEDGFYEVDY NSFHQTFEVP TPVCSARELA
     EASARIDAHL YWSIPSQLDE KVEEEGTEKQ DKQRNGSITS PESEQALSE
//
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