KCIP4_BOVIN
ID KCIP4_BOVIN Reviewed; 250 AA.
AC Q2KI69;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Kv channel-interacting protein 4;
DE Short=KChIP4;
GN Name=KCNIP4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly
CC inactivating A-type potassium channels. Probably modulates channels
CC density, inactivation kinetics and rate of recovery from inactivation
CC in a calcium-dependent and isoform-specific manner. In vitro, modulates
CC KCND2/Kv4.2 and KCND3/Kv4.3 currents (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of heteromultimeric potassium channels. Interacts
CC with KCND2. Interacts with KCND3, and the C-terminus of PSEN2 and
CC probably PSEN1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- DOMAIN: The KIS (K-channel inactivation suppressor) domain is required
CC for converting A-type Kv4 current to a slowly inactivating delayed
CC rectifier potassium current. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; BC112750; AAI12751.1; -; mRNA.
DR RefSeq; NP_001070403.1; NM_001076935.2.
DR AlphaFoldDB; Q2KI69; -.
DR BMRB; Q2KI69; -.
DR SMR; Q2KI69; -.
DR STRING; 9913.ENSBTAP00000054167; -.
DR PaxDb; Q2KI69; -.
DR Ensembl; ENSBTAT00000065041; ENSBTAP00000054167; ENSBTAG00000047743.
DR GeneID; 614299; -.
DR KEGG; bta:614299; -.
DR CTD; 80333; -.
DR VEuPathDB; HostDB:ENSBTAG00000047743; -.
DR VGNC; VGNC:30452; KCNIP4.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000158985; -.
DR HOGENOM; CLU_072366_2_2_1; -.
DR InParanoid; Q2KI69; -.
DR OrthoDB; 1513542at2759; -.
DR TreeFam; TF318560; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000047743; Expressed in occipital lobe and 66 other tissues.
DR ExpressionAtlas; Q2KI69; baseline.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0015459; F:potassium channel regulator activity; IBA:GO_Central.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IBA:GO_Central.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028846; Recoverin.
DR PANTHER; PTHR23055; PTHR23055; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 2: Evidence at transcript level;
KW Calcium; Cell membrane; Ion channel; Ion transport; Membrane;
KW Metal-binding; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Repeat; Transport;
KW Voltage-gated channel.
FT CHAIN 1..250
FT /note="Kv channel-interacting protein 4"
FT /id="PRO_0000245020"
FT DOMAIN 61..117
FT /note="EF-hand 1; degenerate"
FT /evidence="ECO:0000305"
FT DOMAIN 120..155
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 156..191
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 204..239
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 2..44
FT /note="KIS"
FT /evidence="ECO:0000250"
FT REGION 237..250
FT /note="Interaction with KCND2"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PHZ8"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PHZ8"
SQ SEQUENCE 250 AA; 28731 MW; 4EB8B95506486AAF CRC64;
MNVRRVESIS AQLEEASSTG GFLYTQNSTK RSIKERLMKL LPCSAAKTSS PAVQNSVEDE
LEMATVRHRP EALELLEAQS KFTKKELQIL YRGFKNECPS GVVNEDTFKE IYSQFFPQGD
STTYAHFLFN AFDTDHNGAV SFEDFIKGLS ILLRGTVQEK LNWAFNLYDI NKDGYITKEE
MLDIMKAIYD MMGKCTYPVL KEDAPRQHVE TFFQKMDKNK DGVVTIDEFI ESCQKDENIM
RSMQLFENVI
