ID A0A2I2ZL41_GORGO Unreviewed; 426 AA.
AC A0A2I2ZL41;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Potassium calcium-activated channel subfamily N member 3 {ECO:0000313|Ensembl:ENSGGOP00000047937.1};
GN Name=KCNN3 {ECO:0000313|Ensembl:ENSGGOP00000047937.1};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000047937.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000047937.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000047937.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000047937.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CABD030006595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030006596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030006597; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_018878764.1; XM_019023219.1.
DR AlphaFoldDB; A0A2I2ZL41; -.
DR SMR; A0A2I2ZL41; -.
DR Ensembl; ENSGGOT00000050795.1; ENSGGOP00000047937.1; ENSGGOG00000012827.3.
DR GeneID; 101147280; -.
DR CTD; 3782; -.
DR GeneTree; ENSGT00950000182904; -.
DR OrthoDB; 4200919at2759; -.
DR Proteomes; UP000001519; Chromosome 1.
DR Bgee; ENSGGOG00000012827; Expressed in cerebellum and 5 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR GO; GO:0016286; F:small conductance calcium-activated potassium channel activity; IEA:InterPro.
DR Gene3D; 1.10.287.70; -; 2.
DR InterPro; IPR004178; CaM-bd_dom.
DR InterPro; IPR036122; CaM-bd_dom_sf.
DR InterPro; IPR015449; K_chnl_Ca-activ_SK.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR10153; SMALL CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM CHANNEL; 1.
DR PANTHER; PTHR10153:SF40; SMALL CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM CHANNEL PROTEIN 3; 1.
DR Pfam; PF02888; CaMBD; 1.
DR Pfam; PF07885; Ion_trans_2; 1.
DR Pfam; PF03530; SK_channel; 1.
DR SMART; SM01053; CaMBD; 1.
DR SUPFAM; SSF81327; Small-conductance potassium channel; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 4: Predicted;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
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}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 256..332
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000259|SMART:SM01053"
FT REGION 404..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 337..364
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 426 AA; 48050 MW; 1EBE12900FA7719D CRC64;
MERPIKDSMF SLALKCLISL STIILLGLII AYHTREVQLF VIDNGADDWR IAMTYERILY
ISLEMLVCAI HPIPGEYKFF WTARLAFSYT PSRAEADVDI ILSIPMFLRL YLIARVMLLH
SKLFTDASSR SIGALNKINF NTRFVMKTLM TICPGTVLLV FSISLWIIAA WTVRVCERYH
DQQDVTSNFL GAMWLISITF LSIGYGDMVP HTYCGKGVCL LTGIMGAGCT ALVVAVVARK
LELTKAEKHV HNFMMDTQLT KRIKNAAANV LRETWLIYKH TKLLKKIDHA KVRKHQRKFL
QAIHQLRSVK MEQRKLSDQA NTLVDLSKMQ NVMYDLITEL NDRSEDLEKQ IGSLESKLEH
LTASFNSLPL LIADTLRQQQ QQLLSAIIEA RGVSVAVGTT HTPISDSPIG VSSTSFPTPY
TSSSSC
//