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Database: UniProt
Entry: A0A2U3W878_ODORO
LinkDB: A0A2U3W878_ODORO
Original site: A0A2U3W878_ODORO 
ID   A0A2U3W878_ODORO        Unreviewed;       629 AA.
AC   A0A2U3W878;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Potassium voltage-gated channel subfamily D member 2 {ECO:0000256|ARBA:ARBA00017096};
DE   AltName: Full=Voltage-gated potassium channel subunit Kv4.2 {ECO:0000256|ARBA:ARBA00030657};
GN   Name=KCND2 {ECO:0000313|RefSeq:XP_004404463.1};
OS   Odobenus rosmarus divergens (Pacific walrus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC   Odobenus.
OX   NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004404463.1};
RN   [1] {ECO:0000313|RefSeq:XP_004404463.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC       Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004651}. Cell projection, dendrite
CC       {ECO:0000256|ARBA:ARBA00004279}. Cell projection, dendritic spine
CC       {ECO:0000256|ARBA:ARBA00004552}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}. Perikaryon
CC       {ECO:0000256|ARBA:ARBA00004484}. Postsynaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00034100}. Synapse
CC       {ECO:0000256|ARBA:ARBA00034103}. Synaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00034109}.
CC   -!- SIMILARITY: Belongs to the potassium channel family. D (Shal) (TC
CC       1.A.1.2) subfamily. Kv4.2/KCND2 sub-subfamily.
CC       {ECO:0000256|ARBA:ARBA00009309}.
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DR   RefSeq; XP_004404463.1; XM_004404406.2.
DR   AlphaFoldDB; A0A2U3W878; -.
DR   STRING; 9708.A0A2U3W878; -.
DR   GeneID; 101380507; -.
DR   KEGG; oro:101380507; -.
DR   CTD; 3751; -.
DR   InParanoid; A0A2U3W878; -.
DR   OrthoDB; 1478695at2759; -.
DR   Proteomes; UP000245340; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003975; K_chnl_volt-dep_Kv4.
DR   InterPro; IPR004055; K_chnl_volt-dep_Kv4.2.
DR   InterPro; IPR024587; K_chnl_volt-dep_Kv4_C.
DR   InterPro; IPR021645; Shal-type_N.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR003131; T1-type_BTB.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR11537:SF265; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY D MEMBER 2; 1.
DR   PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 1.
DR   Pfam; PF02214; BTB_2; 1.
DR   Pfam; PF11879; DUF3399; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF11601; Shal-type; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01517; KV42CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01497; SHALCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   3: Inferred from homology;
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958};
KW   Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW   Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245340};
KW   Signal {ECO:0000256|SAM:SignalP}; Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..629
FT                   /note="Potassium voltage-gated channel subfamily D member
FT                   2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015768585"
FT   TRANSMEM        183..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        224..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        257..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        324..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        357..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        385..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          41..140
FT                   /note="BTB"
FT                   /evidence="ECO:0000259|SMART:SM00225"
FT   REGION          599..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   629 AA;  70437 MW;  B9D054C3A6B669D9 CRC64;
     MAAGVAAWLP FARAAAIGWM PVASGPMPAP PRQERKRTQD ALIVLNVSGT RFQTWQDTLE
     RYPDTLLGSS ERDFFYHPET QQYFFDRDPD IFRHILNFYR TGKLHYPRHE CISAYDEELA
     FFGLIPEIIG DCCYEEYKDR RRENAERLQD DADTDNTGES TLPTMTARQR VWRAFENPHT
     STMALVFYYV TGFFIAVSVI ANVVETVPCG SSPGHIKELP CGERYAVAFF CLDTACVMIF
     TVEYLLRLAA APSRYRFVRS VMSIIDVVAI LPYYIGLVMT DNEDVSGAFV TLRVFRVFRI
     FKFSRHSQGL RILGYTLKSC ASELGFLLFS LTMAIIIFAT VMFYAEKGSS ASKFTSIPAA
     FWYTIVTMTT LGYGDMVPKT IAGKIFGSIC SLSGVLVIAL PVPVIVSNFS RIYHQNQRAD
     KRRAQKKARL ARIRAAKTGS ANAYMQSKRN GLLSNQLQSS EDEQAFVSKS GSSFETQHHH
     LLHCLEKTTN HEFVDEQVFE ESCTEVATGN RPSSHSPSLS SQGVTSTCCS RRHKKTFRIP
     NANVSGSHRG SVQELSTIQI RCVERTPLSN SRSSLNAKME ECVKLNCEQP YVTTAIISIP
     TPPVTTPEGD DRPESPEYSG GNIVRVSAL
//
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