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Database: UniProt
Entry: U1MBP3_ASCSU
LinkDB: U1MBP3_ASCSU
Original site: U1MBP3_ASCSU 
ID   U1MBP3_ASCSU            Unreviewed;       529 AA.
AC   U1MBP3;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-SEP-2017, entry version 23.
DE   SubName: Full=Potassium voltage-gated channel protein shal {ECO:0000313|EMBL:ERG81763.1};
GN   ORFNames=ASU_09679 {ECO:0000313|EMBL:ERG81763.1};
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Ascaridida;
OC   Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253 {ECO:0000313|EMBL:ERG81763.1, ECO:0000313|Proteomes:UP000017900};
RN   [1] {ECO:0000313|EMBL:ERG81763.1, ECO:0000313|Proteomes:UP000017900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Sperm {ECO:0000313|EMBL:ERG81763.1};
RX   PubMed=21685128; DOI=10.1101/gr.121426.111;
RA   Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA   Davis R.E.;
RT   "Deep small RNA sequencing from the nematode Ascaris reveals
RT   conservation, functional diversification, and novel developmental
RT   profiles.";
RL   Genome Res. 21:1462-1477(2011).
RN   [2] {ECO:0000313|EMBL:ERG81763.1, ECO:0000313|Proteomes:UP000017900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Sperm {ECO:0000313|EMBL:ERG81763.1};
RX   PubMed=23123092; DOI=10.1016/j.devcel.2012.09.020;
RA   Wang J., Mitreva M., Berriman M., Thorne A., Magrini V.,
RA   Koutsovoulos G., Kumar S., Blaxter M.L., Davis R.E.;
RT   "Silencing of germline-expressed genes by DNA elimination in somatic
RT   cells.";
RL   Dev. Cell 23:1072-1080(2012).
CC   -!- SIMILARITY: Belongs to the potassium channel family.
CC       {ECO:0000256|SAAS:SAAS00692852}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ERG81763.1}.
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DR   EMBL; AEUI02000402; ERG81763.1; -; Genomic_DNA.
DR   Proteomes; UP000017900; Unassembled WGS sequence.
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   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; IPR024587; K_chnl_volt-dep_Kv4_C.
DR   InterPro; IPR021645; Shal-type_N.
DR   InterPro; IPR011333; SKP1/BTB/POZ.
DR   InterPro; IPR003131; T1-type_BTB.
DR   InterPro; IPR028325; VG_K_chnl.
DR   PANTHER; PTHR11537; PTHR11537; 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; PR01491; KVCHANNEL.
DR   PRINTS; PR01497; SHALCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000017900};
KW   Ion channel {ECO:0000256|SAAS:SAAS00417203};
KW   Ion transport {ECO:0000256|SAAS:SAAS00417186};
KW   Membrane {ECO:0000256|SAAS:SAAS00788393, ECO:0000256|SAM:Phobius};
KW   Potassium {ECO:0000256|SAAS:SAAS00417282};
KW   Potassium channel {ECO:0000256|SAAS:SAAS00417246};
KW   Potassium transport {ECO:0000256|SAAS:SAAS00417240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017900};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00793138,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00789957,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00417268};
KW   Voltage-gated channel {ECO:0000256|SAAS:SAAS00091688}.
FT   TRANSMEM    189    207       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    259    277       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    315    336       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       46    145       BTB. {ECO:0000259|SMART:SM00225}.
SQ   SEQUENCE   529 AA;  59457 MW;  8A6C7FB05C0D34A5 CRC64;
     MASVAAWLPF ARAAAIGWVP ISRQPMPTAP IAIQAKDLAV DHVSDEKLSI NISGRRFETW
     RNTLEKFPET LLGSNEKEFF YDEDTCEYFF DRDPDIFRHI LTFYRTGKLH YPKHECLVAY
     DEELSFFGIM PDLISDCCYE DYKDKKRENQ ERVMEERLDT ADKAKRTLSL QQKMWAAFEN
     PHTSSVALVF YYVTGFFIAV SVLCNIIETV PCKYMADDAT VSCGDLYERQ FFVLDTACVI
     IFTVEYLARL FAAPDRCKFL RSIMSVIDVV AILPYYVGLG LTNNKDVSGA FVTLRVFMTT
     LGYGDMVPAT IMGKVVGGVC SLSGVLVIAL PVPVIVSNFS RIYHQNQRAD KRKAQKKARL
     ARIRIVKNAS GQALFSKKKA HEARMQAFEE GTLSLDALKD EDIFEIQHHH LLQCLERATE
     RELVETDIAF DGGMKPTPPL SLSTSHENLH SSGTRAGFIG CCPFRIGRQR DCGVGHVSFV
     TDTDDRPADA GGGGRDEWSS RDGDQRTHLP FKRHIAEGNA PTNICISSL
//
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