KCIP4_MOUSE
ID KCIP4_MOUSE Reviewed; 250 AA.
AC Q6PHZ8; Q6DTJ3; Q8CAD0; Q8R4I2; Q9EQ01;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Kv channel-interacting protein 4;
DE Short=KChIP4;
DE AltName: Full=A-type potassium channel modulatory protein 4;
DE AltName: Full=Calsenilin-like protein;
DE AltName: Full=Potassium channel-interacting protein 4;
GN Name=Kcnip4; Synonyms=Calp, Kchip4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11847232; DOI=10.1074/jbc.m200897200;
RA Morohashi Y., Hatano N., Ohya S., Takikawa R., Watabiki T., Takasugi N.,
RA Imaizumi Y., Tomita T., Iwatsubo T.;
RT "Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand
RT protein interacting with presenilin 2 and voltage-gated potassium channel
RT subunit Kv4.";
RL J. Biol. Chem. 277:14965-14975(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, TISSUE SPECIFICITY,
RP DOMAIN, AND INTERACTION WITH KCND2.
RC STRAIN=C57BL/6J;
RX PubMed=11805342; DOI=10.1073/pnas.022509299;
RA Holmqvist M.H., Cao J., Hernandez-Pineda R., Jacobson M.D., Carroll K.I.,
RA Sung M.A., Betty M., Ge P., Gilbride K.J., Brown M.E., Jurman M.E.,
RA Lawson D., Silos-Santiago I., Xie Y., Covarrubias M., Rhodes K.J.,
RA Distefano P.S., An W.F.;
RT "Elimination of fast inactivation in Kv4 A-type potassium channels by an
RT auxiliary subunit domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:1035-1040(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Xia K.U., Fang H.Y., Zhong X.Y., Xia J.H., Zhang Z.H.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-192 (ISOFORM 2).
RC TISSUE=Retina;
RA Ida H., Boylan S., Weigel A., Smit-McBride Z., Chao A., Gao J., Buchoff P.,
RA Wistow G., Hjelmeland L.;
RT "Expressed sequence tag analysis of mouse retina.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=15363885; DOI=10.1016/j.molbrainres.2004.06.024;
RA Xiong H., Kovacs I., Zhang Z.;
RT "Differential distribution of KChIPs mRNAs in adult mouse brain.";
RL Brain Res. Mol. Brain Res. 128:103-111(2004).
RN [8]
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19713751; DOI=10.4161/chan.3.4.9553;
RA Marionneau C., LeDuc R.D., Rohrs H.W., Link A.J., Townsend R.R.,
RA Nerbonne J.M.;
RT "Proteomic analyses of native brain K(V)4.2 channel complexes.";
RL Channels 3:284-294(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-56, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP INTERACTION WITH KCND2, AND FUNCTION.
RX PubMed=20943905; DOI=10.1523/jneurosci.2487-10.2010;
RA Norris A.J., Foeger N.C., Nerbonne J.M.;
RT "Interdependent roles for accessory KChIP2, KChIP3, and KChIP4 subunits in
RT the generation of Kv4-encoded IA channels in cortical pyramidal neurons.";
RL J. Neurosci. 30:13644-13655(2010).
RN [11]
RP FUNCTION, AND INTERACTION WITH KCND2.
RX PubMed=20045463; DOI=10.1016/j.mcn.2009.12.005;
RA Lin L., Sun W., Wikenheiser A.M., Kung F., Hoffman D.A.;
RT "KChIP4a regulates Kv4.2 channel trafficking through PKA phosphorylation.";
RL Mol. Cell. Neurosci. 43:315-325(2010).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 56-250 IN COMPLEX WITH CALCIUM
RP IONS, INTERACTION WITH KCND3/KV4.3, AND FUNCTION.
RX PubMed=19109250; DOI=10.1074/jbc.m807704200;
RA Liang P., Wang H., Chen H., Cui Y., Gu L., Chai J., Wang K.;
RT "Structural insights into KChIP4a modulation of Kv4.3 inactivation.";
RL J. Biol. Chem. 284:4960-4967(2009).
CC -!- FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly
CC inactivating A-type potassium channels, such as KCND2/Kv4.2 and
CC KCND3/Kv4.3 (PubMed:19109250). Modulates channel expression at the cell
CC membrane, gating characteristics, inactivation kinetics and rate of
CC recovery from inactivation in a calcium-dependent and isoform-specific
CC manner. {ECO:0000269|PubMed:19109250, ECO:0000269|PubMed:20045463,
CC ECO:0000269|PubMed:20943905}.
CC -!- SUBUNIT: Component of heteromultimeric potassium channels
CC (PubMed:19713751, PubMed:20943905). Identified in potassium channel
CC complexes containing KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3,
CC KCNIP4, DPP6 and DPP10 (PubMed:19713751). Interacts with the C-terminus
CC of PSEN2 and probably PSEN1 (By similarity). Interacts with KCND2 and
CC KCND3. {ECO:0000250|UniProtKB:Q6PIL6, ECO:0000269|PubMed:11805342,
CC ECO:0000269|PubMed:19109250, ECO:0000269|PubMed:20045463,
CC ECO:0000269|PubMed:20943905}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6PIL6};
CC Peripheral membrane protein {ECO:0000305}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q6PIL6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6PHZ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PHZ8-2; Sequence=VSP_015071;
CC Name=3;
CC IsoId=Q6PHZ8-3; Sequence=VSP_015069;
CC Name=4; Synonyms=KChIPa;
CC IsoId=Q6PHZ8-4; Sequence=VSP_015070;
CC -!- TISSUE SPECIFICITY: Expressed in brain. Highly expressed by neurons in
CC layers II-IV of cortex and in hippocampus, thalamus and the Purkinje
CC cell layer of the cerebellum. {ECO:0000269|PubMed:11805342,
CC ECO:0000269|PubMed:11847232, ECO:0000269|PubMed:15363885}.
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:0000269|PubMed:11805342}.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; AF305071; AAG36976.1; -; mRNA.
DR EMBL; AF453243; AAL86766.1; -; mRNA.
DR EMBL; AY647240; AAT68466.1; -; mRNA.
DR EMBL; AK039048; BAC30218.1; -; mRNA.
DR EMBL; BC051130; AAH51130.1; -; mRNA.
DR EMBL; CK618709; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS39084.1; -. [Q6PHZ8-4]
DR CCDS; CCDS57341.1; -. [Q6PHZ8-2]
DR CCDS; CCDS57342.1; -. [Q6PHZ8-1]
DR RefSeq; NP_001186171.1; NM_001199242.1. [Q6PHZ8-1]
DR RefSeq; NP_001186172.1; NM_001199243.1. [Q6PHZ8-2]
DR RefSeq; NP_084541.3; NM_030265.3. [Q6PHZ8-4]
DR PDB; 3DD4; X-ray; 3.00 A; A=56-250.
DR PDBsum; 3DD4; -.
DR AlphaFoldDB; Q6PHZ8; -.
DR BMRB; Q6PHZ8; -.
DR SMR; Q6PHZ8; -.
DR BioGRID; 219785; 2.
DR STRING; 10090.ENSMUSP00000134758; -.
DR iPTMnet; Q6PHZ8; -.
DR PhosphoSitePlus; Q6PHZ8; -.
DR MaxQB; Q6PHZ8; -.
DR PaxDb; Q6PHZ8; -.
DR PRIDE; Q6PHZ8; -.
DR ProteomicsDB; 263585; -. [Q6PHZ8-1]
DR ProteomicsDB; 263586; -. [Q6PHZ8-2]
DR ProteomicsDB; 263587; -. [Q6PHZ8-3]
DR ProteomicsDB; 263588; -. [Q6PHZ8-4]
DR ABCD; Q6PHZ8; 2 sequenced antibodies.
DR Antibodypedia; 10064; 199 antibodies from 25 providers.
DR DNASU; 80334; -.
DR Ensembl; ENSMUST00000087395; ENSMUSP00000084656; ENSMUSG00000029088. [Q6PHZ8-1]
DR Ensembl; ENSMUST00000176191; ENSMUSP00000135071; ENSMUSG00000029088. [Q6PHZ8-2]
DR Ensembl; ENSMUST00000176978; ENSMUSP00000134758; ENSMUSG00000029088. [Q6PHZ8-4]
DR GeneID; 80334; -.
DR KEGG; mmu:80334; -.
DR UCSC; uc033ijo.1; mouse. [Q6PHZ8-1]
DR CTD; 80333; -.
DR MGI; MGI:1933131; Kcnip4.
DR VEuPathDB; HostDB:ENSMUSG00000029088; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000158985; -.
DR HOGENOM; CLU_072366_2_2_1; -.
DR InParanoid; Q6PHZ8; -.
DR PhylomeDB; Q6PHZ8; -.
DR TreeFam; TF318560; -.
DR Reactome; R-MMU-5576894; Phase 1 - inactivation of fast Na+ channels.
DR BioGRID-ORCS; 80334; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Kcnip4; mouse.
DR EvolutionaryTrace; Q6PHZ8; -.
DR PRO; PR:Q6PHZ8; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6PHZ8; protein.
DR Bgee; ENSMUSG00000029088; Expressed in medial dorsal nucleus of thalamus and 159 other tissues.
DR ExpressionAtlas; Q6PHZ8; baseline and differential.
DR Genevisible; Q6PHZ8; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0015459; F:potassium channel regulator activity; IMP:UniProtKB.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IMP: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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell membrane; Cytoplasm;
KW Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Repeat; Transport; Voltage-gated channel.
FT CHAIN 1..250
FT /note="Kv channel-interacting protein 4"
FT /id="PRO_0000073827"
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 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 ECO:0000269|PubMed:19109250"
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 ECO:0000269|PubMed:19109250"
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 ECO:0000269|PubMed:19109250"
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 ECO:0000269|PubMed:19109250"
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 ECO:0000269|PubMed:19109250"
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 ECO:0000269|PubMed:19109250"
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 ECO:0000269|PubMed:19109250"
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 ECO:0000269|PubMed:19109250"
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 ECO:0000269|PubMed:19109250"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..62
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_015069"
FT VAR_SEQ 1..55
FT /note="MNVRRVESISAQLEEASSTGGFLYAQNNTKRSIKERLMKLLPCSAAKTSSPA
FT IQN -> MNLEGLEMIAVLIVIVLFVKLLEQFGLIEAGLED (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11805342,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_015070"
FT VAR_SEQ 21..55
FT /note="GFLYAQNNTKRSIKERLMKLLPCSAAKTSSPAIQN -> D (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_015071"
FT CONFLICT 32
FT /note="S -> T (in Ref. 1; AAG36976)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="R -> K (in Ref. 4; BAC30218)"
FT /evidence="ECO:0000305"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:3DD4"
FT HELIX 69..95
FT /evidence="ECO:0007829|PDB:3DD4"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:3DD4"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3DD4"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:3DD4"
FT HELIX 142..154
FT /evidence="ECO:0007829|PDB:3DD4"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:3DD4"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:3DD4"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:3DD4"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:3DD4"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:3DD4"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:3DD4"
SQ SEQUENCE 250 AA; 28756 MW; 56542298021192BF CRC64;
MNVRRVESIS AQLEEASSTG GFLYAQNNTK RSIKERLMKL LPCSAAKTSS PAIQNSVEDE
LEMATVRHRP EALELLEAQS KFTKKELQIL YRGFKNECPS GVVNEETFKE IYSQFFPQGD
STTYAHFLFN AFDTDHNGAV SFEDFIKGLS ILLRGTVQEK LNWAFNLYDI NKDGYITKEE
MLDIMKAIYD MMGKCTYPVL KEDAPRQHVE TFFQKMDKNK DGVVTIDEFI ESCQKDENIM
RSMQLFENVI
