KCIP2_MUSPF
ID KCIP2_MUSPF Reviewed; 270 AA.
AC Q8WN03; Q8WN04; Q8WN05;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Kv channel-interacting protein 2;
DE Short=KChIP2;
DE AltName: Full=A-type potassium channel modulatory protein 2;
DE AltName: Full=Potassium channel-interacting protein 2;
GN Name=Kcnip2; Synonyms=Kchip2;
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC Mustela.
OX NCBI_TaxID=9669;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=11897837; DOI=10.1113/jphysiol.2001.015156;
RA Patel S.P., Campbell D.L., Morales M.J., Strauss H.C.;
RT "Heterogeneous expression of KChIP2 isoforms in the ferret heart.";
RL J. Physiol. (Lond.) 539:649-656(2002).
CC -!- FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly
CC inactivating A-type potassium channels. Modulates channel density,
CC inactivation kinetics and rate of recovery from inactivation in a
CC calcium-dependent and isoform-specific manner. In vitro, modulates
CC KCND2/Kv4.2 and KCND3/Kv4.3 currents. Involved in KCND2 and KCND3
CC trafficking to the cell surface. Essential for the expression of I(To)
CC currents in the heart. Required for normal protein levels of KCND2 in
CC the heart ventricle (By similarity). {ECO:0000250|UniProtKB:Q9JJ69,
CC ECO:0000250|UniProtKB:Q9NS61}.
CC -!- SUBUNIT: Component of heteromultimeric potassium channels. Identified
CC in potassium channel complexes containing KCND1, KCND2, KCND3, KCNIP1,
CC KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (By similarity). The KCND2-
CC KCNIP2 channel complex contains four KCND2 and four KCNIP2 subunits.
CC Probably part of a complex consisting of KCNIP1, KCNIP2 isoform 3 and
CC KCND2. At least isoform 2 and isoform 3 can self-associate to form
CC homodimers and homotetramers. Isoform 3 interacts with KCNIP1 in a
CC calcium-dependent manner (By similarity). Interacts with KCND2. Isoform
CC 1 and isoform 3 interact with KCND3 isoform 1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9JJ69, ECO:0000250|UniProtKB:Q9NS61}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9JM59};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q9JM59}. Note=Detected on lipid
CC rafts (By similarity). {ECO:0000250|UniProtKB:Q9JM59}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=KChip2b;
CC IsoId=Q8WN03-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WN03-2; Sequence=VSP_015063;
CC Name=3; Synonyms=KChip2a;
CC IsoId=Q8WN03-3; Sequence=VSP_015062;
CC -!- TISSUE SPECIFICITY: Expressed in heart ventricle with isoform 1 as most
CC prominent form. {ECO:0000269|PubMed:11897837}.
CC -!- PTM: Palmitoylated. Palmitoylation enhances association with the plasma
CC membrane. {ECO:0000250|UniProtKB:Q9JM59}.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; AF454385; AAL51035.1; -; mRNA.
DR EMBL; AF454386; AAL51036.1; -; mRNA.
DR EMBL; AF454387; AAL51037.1; -; mRNA.
DR RefSeq; XP_004749481.1; XM_004749424.2. [Q8WN03-1]
DR RefSeq; XP_004749484.1; XM_004749427.2. [Q8WN03-2]
DR RefSeq; XP_004749487.1; XM_004749430.2. [Q8WN03-3]
DR AlphaFoldDB; Q8WN03; -.
DR SMR; Q8WN03; -.
DR STRING; 9669.ENSMPUP00000016787; -.
DR Ensembl; ENSMPUT00000017037; ENSMPUP00000016788; ENSMPUG00000016892. [Q8WN03-3]
DR GeneID; 101686160; -.
DR KEGG; mpuf:101686160; -.
DR CTD; 30819; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000157798; -.
DR HOGENOM; CLU_072366_2_2_1; -.
DR InParanoid; Q8WN03; -.
DR Proteomes; UP000000715; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISS:UniProtKB.
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 Alternative splicing; Calcium; Cell membrane; Ion channel; Ion transport;
KW Lipoprotein; Membrane; Metal-binding; Palmitate; Phosphoprotein; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Repeat;
KW Transport; Voltage-gated channel.
FT CHAIN 1..270
FT /note="Kv channel-interacting protein 2"
FT /id="PRO_0000073823"
FT DOMAIN 81..137
FT /note="EF-hand 1; degenerate"
FT /evidence="ECO:0000305"
FT DOMAIN 140..175
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 176..211
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 224..259
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..270
FT /note="Interaction with KCND2"
FT /evidence="ECO:0000250|UniProtKB:Q8R426"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM59"
FT LIPID 45
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM59"
FT LIPID 46
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM59"
FT VAR_SEQ 25..74
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11897837"
FT /id="VSP_015062"
FT VAR_SEQ 57..75
FT /note="TLAVPASLRPHRPRPLDPD -> N (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11897837"
FT /id="VSP_015063"
SQ SEQUENCE 270 AA; 30947 MW; 24D7E583F3613E82 CRC64;
MRGQGRKESL SDSRDLDGSY DQLTGHPPGP TKKALKQRFL KLLPCCGPQA LPSVSETLAV
PASLRPHRPR PLDPDSVEDE FELSTVCHRP EGLEQLQEQT KFTRKELQVL YRGFKNECPS
GIVNEENFKQ IYSQFFPQGD SSTYATFLFN AFDTNHDGSV SFEDFVAGLS VILRGTIDDR
LNWAFNLYDL NKDGCITKEE MLDIMKSIYD MMGKYTYPAL REEAPREHVE SFFQKMDRNK
DGVVTIEEFI ESCQKDENIM RSMQLFDNVI
