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KCNT1_CHICK
ID   KCNT1_CHICK             Reviewed;        1201 AA.
AC   Q8QFV0;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Potassium channel subfamily T member 1;
DE   AltName: Full=Sequence like a calcium-activated potassium channel subunit;
GN   Name=KCNT1; Synonyms=SLACK;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Forebrain;
RA   Li M., Caruso L., Bell T., Tu T., Oberholtzer J.C.;
RT   "Cloning and characterization of potassium channel subunit (slack) from
RT   chick brain.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Generates outwardly rectifying currents that are suppressed
CC       by elevation of intracellular calcium. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the potassium channel family. Calcium-activated
CC       (TC 1.A.1.3) subfamily. KCa4.1/KCNT1 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AY093434; AAM18770.1; -; mRNA.
DR   RefSeq; NP_989893.1; NM_204562.2.
DR   PDB; 5A6E; EM; 4.50 A; B=244-337, C=351-1019, C=1141-1171.
DR   PDB; 5A6F; EM; 4.20 A; C=351-1019, C=1141-1171.
DR   PDB; 5A6G; EM; 4.50 A; B=244-337.
DR   PDB; 5U70; EM; 3.70 A; A=1-1201.
DR   PDB; 5U76; EM; 4.20 A; A=1-1201.
DR   PDBsum; 5A6E; -.
DR   PDBsum; 5A6F; -.
DR   PDBsum; 5A6G; -.
DR   PDBsum; 5U70; -.
DR   PDBsum; 5U76; -.
DR   AlphaFoldDB; Q8QFV0; -.
DR   SMR; Q8QFV0; -.
DR   DIP; DIP-61789N; -.
DR   STRING; 9031.ENSGALP00000038129; -.
DR   PaxDb; Q8QFV0; -.
DR   Ensembl; ENSGALT00000038919; ENSGALP00000038129; ENSGALG00000001645.
DR   GeneID; 395248; -.
DR   KEGG; gga:395248; -.
DR   CTD; 57582; -.
DR   VEuPathDB; HostDB:geneid_395248; -.
DR   eggNOG; KOG3193; Eukaryota.
DR   GeneTree; ENSGT00940000156880; -.
DR   HOGENOM; CLU_003370_0_0_1; -.
DR   InParanoid; Q8QFV0; -.
DR   OrthoDB; 858812at2759; -.
DR   PhylomeDB; Q8QFV0; -.
DR   PRO; PR:Q8QFV0; -.
DR   Proteomes; UP000000539; Chromosome 17.
DR   Bgee; ENSGALG00000001645; Expressed in cerebellum and 1 other tissue.
DR   ExpressionAtlas; Q8QFV0; baseline.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005228; F:intracellular sodium activated potassium channel activity; IBA:GO_Central.
DR   GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central.
DR   InterPro; IPR003929; K_chnl_BK_asu.
DR   InterPro; IPR013099; K_chnl_dom.
DR   Pfam; PF03493; BK_channel_a; 1.
DR   Pfam; PF07885; Ion_trans_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cell membrane; Glycoprotein; Ion channel;
KW   Ion transport; Membrane; Potassium; Potassium channel; Potassium transport;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1201
FT                   /note="Potassium channel subfamily T member 1"
FT                   /id="PRO_0000054093"
FT   TOPO_DOM        1..95
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        117..153
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        154..174
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        175..185
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..206
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        207..211
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..224
FT                   /note="Helical; Name=Segment S4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        225..249
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        250..270
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        271..279
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        280..300
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        301..302
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        324..1201
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          473..594
FT                   /note="RCK N-terminal"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1175..1201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1178..1201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1201 AA;  137242 MW;  18E18FE0CFF26E20 CRC64;
     MARAKLKNSP SESNSHVKTV PPATTEDVRG VSPLLPARRM GSLGSDVGQR PHAEDFSMDS
     SFSQVQVEFY VNENTFKERL KLFFIKNQRS SLRIRLFNFS LKLLTCLLYI VRVLLDNPEE
     GIGCWECEKQ NYTLFNQSTK INWSHIFWVD RKLPLWAVQV SIALISFLET MLLIYLSYKG
     NIWEQIFRIS FILEMINTVP FIITIFWPPL RNLFIPVFLN CWLAKYALEN MINDLHRAIQ
     RTQSAMFNQV LILICTLLCL VFTGTCGIQH LERAGEKLSL FKSFYFCIVT FSTVGYGDVT
     PKIWPSQLLV VIMICVALVV LPLQFEELVY LWMERQKSGG NYSRHRAQTE KHVVLCVSSL
     KIDLLMDFLN EFYAHPRLQD YYVVILCPTE MDIQVRRVLQ IPLWSQRVIY LQGSALKDQD
     LMRAKMDNGE ACFILSSRNE VDRTAADHQT ILRAWAVKDF APNCPLYVQI LKPENKFHVK
     FADHVVCEEE CKYAMLALNC VCPATSTLIT LLVHTSRGQE GQESPEQWQR MYGRCSGNEV
     YHIRMGDSKF FMEYEGKSFT YAAFHAHKKY GVCLIGIRRE ENKSILLNPG PRHIMAASDT
     CFYINITKEE NSAFIFKQAE KQKKKGFAGR GTYDGPSRLP VHSIIASMGT VAMDLQNTEC
     RPTNSSKLAL PAENGSGNRR PSIAPVLELA DTSSLLPCDL LSDQSEDEMT QSDEEGSAVV
     EYVKGYPPNS PYIGSSPTLC HLLPEKAPFC CLRLDKGCKH NSFEDAKAYG FKNKLIIVSA
     ETAGNGLYNF IVPLRAYYRS RKELNPIVLL LDNKPEHHFL EAICCFPMVY YMEGTIDNLD
     SLLQCGIIYA DNLVVVDKES TMSAEEDYMA DAKTIVNVQT MFRLFPSLSI ITELTHPSNM
     RFMQFRAKDS YSLALSKLEK KERENGSNLA FMFRLPFAAG RVFSISMLDT LLYQSFVKDY
     MITITRLLLG LDTTPGSGYL CAMKITEDDL WIRTYGRLFQ KLCSSSAEIP IGIYRTESHM
     FATSEPHDIR AQSQISINVE DCEDTKDVKE HWGIKTGHHR NSCSSDQSEH PLLRRKSMQW
     ARRLSRKGNK HSGKTAEWIS QQRLSLYRRS ERQELSELVK NRMKHLGLPT TGYDEMNDHQ
     NTLSYVLINP PPDTRLELND IVYLIRSDPL AHVANDGHSR KSSCSNKLGP CNPETRDETQ
     L
 
 
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