ID   TRPM4_RAT               Reviewed;        1208 AA.
AC   Q9ESQ5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=Transient receptor potential cation channel subfamily M member 4;
DE   AltName: Full=Calcium-activated non-selective cation channel 1;
DE   AltName: Full=Long transient receptor potential channel 4;
DE            Short=LTrpC-4;
DE            Short=LTrpC4;
DE   AltName: Full=MLS2s;
DE   AltName: Full=Melastatin-like 2;
GN   Name=Trpm4; Synonyms=Ltrpc4;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=19945433; DOI=10.1016/j.bbrc.2009.11.142;
RA   Yoo J.C., Yarishkin O.V., Hwang E.M., Kim E., Kim D.G., Park N., Hong S.G.,
RA   Park J.Y.;
RT   "Cloning and characterization of rat transient receptor potential-
RT   melastatin 4 (TRPM4).";
RL   Biochem. Biophys. Res. Commun. 391:806-811(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 717-1208.
RC   TISSUE=Brain;
RA   Ohki G., Ishibashi K., Suzuki M.;
RT   "Cloning of novel Ca-permeable channels.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION.
RX   PubMed=15030426; DOI=10.1046/j.1540-8167.2004.03477.x;
RA   Guinamard R., Chatelier A., Lenfant J., Bois P.;
RT   "Activation of the Ca(2+)-activated nonselective cation channel by
RT   diacylglycerol analogues in rat cardiomyocytes.";
RL   J. Cardiovasc. Electrophysiol. 15:342-348(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=16966582; DOI=10.1161/01.hyp.0000237864.65019.a5;
RA   Guinamard R., Demion M., Magaud C., Potreau D., Bois P.;
RT   "Functional expression of the TRPM4 cationic current in ventricular
RT   cardiomyocytes from spontaneously hypertensive rats.";
RL   Hypertension 48:587-594(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Calcium-activated non selective (CAN) cation channel that
CC       mediates membrane depolarization. While it is activated by increase in
CC       intracellular Ca(2+), it is impermeable to it. Mediates transport of
CC       monovalent cations (Na(+) > K(+) > Cs(+) > Li(+)), leading to
CC       depolarize the membrane. It thereby plays a central role in
CC       cadiomyocytes, neurons from entorhinal cortex, dorsal root and
CC       vomeronasal neurons, endocrine pancreas cells, kidney epithelial cells,
CC       cochlea hair cells etc. Participates in T-cell activation by modulating
CC       Ca(2+) oscillations after T lymphocyte activation, which is required
CC       for NFAT-dependent IL2 production. Involved in myogenic constriction of
CC       cerebral arteries. Controls insulin secretion in pancreatic beta-cells.
CC       May also be involved in pacemaking or could cause irregular electrical
CC       activity under conditions of Ca(2+) overload. Affects T-helper 1 (Th1)
CC       and T-helper 2 (Th2) cell motility and cytokine production through
CC       differential regulation of calcium signaling and NFATC1 localization.
CC       Enhances cell proliferation through up-regulation of the beta-catenin
CC       signaling pathway. Essential for the migration but not the maturation
CC       of dendritic cells (By similarity). Plays a role in keratinocyte
CC       differentiation (By similarity). {ECO:0000250|UniProtKB:Q7TN37,
CC       ECO:0000250|UniProtKB:Q8TD43, ECO:0000269|PubMed:16966582,
CC       ECO:0000269|PubMed:19945433}.
CC   -!- ACTIVITY REGULATION: Gating is voltage-dependent and repressed by
CC       decavanadate. Calmodulin-binding confers the Ca(2+) sensitivity. ATP is
CC       able to restore Ca(2+) sensitivity after desensitization.
CC       Phosphatidylinositol 4,5-bisphosphate (PIP2)-binding strongly enhances
CC       activity, by increasing the channel's Ca(2+) sensitivity and shifting
CC       its voltage dependence of activation towards negative potentials.
CC       Activity is also enhanced by 3,5-bis(trifluoromethyl)pyrazole
CC       derivative (BTP2) (By similarity). {ECO:0000250|UniProtKB:Q8TD43}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q8TD43}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC       {ECO:0000269|PubMed:19945433}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q8TD43}. Endoplasmic reticulum
CC       {ECO:0000269|PubMed:19945433}. Golgi apparatus
CC       {ECO:0000269|PubMed:19945433}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC       {ECO:0000269|PubMed:19945433}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q8TD43}. Endoplasmic reticulum
CC       {ECO:0000269|PubMed:19945433}. Golgi apparatus
CC       {ECO:0000269|PubMed:19945433}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms may exist.;
CC       Name=1; Synonyms=TRPM4b;
CC         IsoId=Q9ESQ5-1; Sequence=Displayed;
CC       Name=2; Synonyms=TRPM4a;
CC         IsoId=Q9ESQ5-2; Sequence=VSP_040337;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in the testis with a
CC       moderate expression in the brain, spleen and thymus. Isoform 2 is only
CC       expressed in the brain and spleen. {ECO:0000269|PubMed:19945433}.
CC   -!- PTM: Phosphorylation by PKC leads to increase the sensitivity to
CC       Ca(2+). {ECO:0000250|UniProtKB:Q8TD43}.
CC   -!- PTM: Sumoylated. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q8TD43}.
CC   -!- MISCELLANEOUS: [Isoform 2]: Probably non-functional. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. LTrpC
CC       subfamily. TRPM4 sub-subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB15808.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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DR   EMBL; AABR03000917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03004552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB040807; BAB15808.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001129701.1; NM_001136229.1. [Q9ESQ5-1]
DR   AlphaFoldDB; Q9ESQ5; -.
DR   SMR; Q9ESQ5; -.
DR   STRING; 10116.ENSRNOP00000041387; -.
DR   iPTMnet; Q9ESQ5; -.
DR   PhosphoSitePlus; Q9ESQ5; -.
DR   PaxDb; 10116-ENSRNOP00000041387; -.
DR   ABCD; Q9ESQ5; 1 sequenced antibody.
DR   GeneID; 171143; -.
DR   KEGG; rno:171143; -.
DR   UCSC; RGD:620244; rat. [Q9ESQ5-1]
DR   AGR; RGD:620244; -.
DR   CTD; 54795; -.
DR   RGD; 620244; Trpm4.
DR   eggNOG; KOG3614; Eukaryota.
DR   HOGENOM; CLU_001390_0_3_1; -.
DR   InParanoid; Q9ESQ5; -.
DR   OrthoDB; 201873at2759; -.
DR   PhylomeDB; Q9ESQ5; -.
DR   TreeFam; TF314204; -.
DR   Reactome; R-RNO-3295583; TRP channels.
DR   PRO; PR:Q9ESQ5; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0034706; C:sodium channel complex; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; ISO:RGD.
DR   GO; GO:0005262; F:calcium channel activity; ISO:RGD.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0005227; F:calcium-activated cation channel activity; IDA:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0099604; F:ligand-gated calcium channel activity; IBA:GO_Central.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR   GO; GO:0019722; P:calcium-mediated signaling; ISO:RGD.
DR   GO; GO:0071318; P:cellular response to ATP; ISO:RGD.
DR   GO; GO:0002407; P:dendritic cell chemotaxis; ISS:UniProtKB.
DR   GO; GO:0098662; P:inorganic cation transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0007616; P:long-term memory; IMP:RGD.
DR   GO; GO:0086045; P:membrane depolarization during AV node cell action potential; ISO:RGD.
DR   GO; GO:0086048; P:membrane depolarization during bundle of His cell action potential; ISO:RGD.
DR   GO; GO:0086047; P:membrane depolarization during Purkinje myocyte cell action potential; ISO:RGD.
DR   GO; GO:0030502; P:negative regulation of bone mineralization; IMP:RGD.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:RGD.
DR   GO; GO:1904179; P:positive regulation of adipose tissue development; IMP:RGD.
DR   GO; GO:1903949; P:positive regulation of atrial cardiac muscle cell action potential; IMP:RGD.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
DR   GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:RGD.
DR   GO; GO:0010460; P:positive regulation of heart rate; IMP:RGD.
DR   GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:RGD.
DR   GO; GO:1904199; P:positive regulation of regulation of vascular associated smooth muscle cell membrane depolarization; IMP:RGD.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR   GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:RGD.
DR   GO; GO:0002724; P:regulation of T cell cytokine production; ISS:UniProtKB.
DR   GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; ISO:RGD.
DR   GO; GO:0098719; P:sodium ion import across plasma membrane; ISO:RGD.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR041491; TRPM_SLOG.
DR   PANTHER; PTHR13800:SF6; TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY M MEMBER 4; 1.
DR   PANTHER; PTHR13800; TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL, SUBFAMILY M, MEMBER 6; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF18139; LSDAT_euk; 1.
DR   SUPFAM; SSF140860; Pseudo ankyrin repeat-like; 1.
DR   Genevisible; Q9ESQ5; RN.
PE   1: Evidence at protein level;
KW   Adaptive immunity; Alternative splicing; ATP-binding; Calcium;
KW   Calmodulin-binding; Cell membrane; Coiled coil; Disulfide bond;
KW   Endoplasmic reticulum; Golgi apparatus; Immunity; Ion channel;
KW   Ion transport; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW   Ubl conjugation.
FT   CHAIN           1..1208
FT                   /note="Transient receptor potential cation channel
FT                   subfamily M member 4"
FT                   /id="PRO_0000259531"
FT   TOPO_DOM        1..776
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   TRANSMEM        777..797
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   TOPO_DOM        798..808
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   TRANSMEM        809..829
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   TOPO_DOM        830..857
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   TRANSMEM        858..878
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   TOPO_DOM        879..880
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   TRANSMEM        881..904
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   TOPO_DOM        905..924
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   TRANSMEM        925..945
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   TOPO_DOM        946..957
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   INTRAMEM        958..978
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   TOPO_DOM        979..1013
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   TRANSMEM        1014..1034
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   TOPO_DOM        1035..1208
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   REGION          1070..1170
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          1130..1135
FT                   /note="Mediates modulation by decavanadate and PIP2-
FT                   binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT   REGION          1189..1208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1128..1180
FT                   /evidence="ECO:0000255"
FT   MOTIF           969..971
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   COMPBIAS        1193..1208
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         172
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   BINDING         422
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   BINDING         449
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   BINDING         822
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT   BINDING         825
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT   BINDING         859
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT   BINDING         862
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT   MOD_RES         527
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         538
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   MOD_RES         1139
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT   MOD_RES         1146
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT   DISULFID        987..1005
FT                   /evidence="ECO:0000250|UniProtKB:Q7TN37"
FT   VAR_SEQ         1..186
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:19945433"
FT                   /id="VSP_040337"
SQ   SEQUENCE   1208 AA;  135341 MW;  324CEC9A6B9F7EA6 CRC64;
     MVGQEKEQSW IPKIFRKKVC TTFIVDLHDD AGGTLCQCGQ PRDAHPSVAV EDAFGAAVVT
     EWNSDEHTTE KPTDAYGDLD FTYSGRKSSN FLRLSDRTDP ATVYSLVTRS WGFRAPNLVV
     SVLGGSEGPV LQTWLQDLLR RGLVRAAQST GAWIVTGGLH TGIGRHVGVA VRDHQTASTG
     GSKVVAMGVA PWGVVRNRDM LINPKGSFPA RYRWRGDPED GVEFPLDYNY SAFFLVDDGT
     YGRMGGENRF RLRFESYVAQ QKTGVGGTGI DIPVLLLLIE GDEKMLKRIE DATQAQLPCL
     LVAGSGGAAD CLVETLEDTL APGSGGLRRG EARDRIRRYF PKGDPEVLQA QVERIMTRKE
     LLTVYSSEDG SEEFETIVLR ALVKACGSSE ASAYLDELRL AVAWNRVDIA QSELFRGDIQ
     WRSFHLEASL MDALLNDRPE FVRLLISHGL SLGHFLTPVR LAQLYSAVSP NSLIRNLLDQ
     ASHASSSKSP PANGAAELRP PNVGQVLRTL LGETCAPRYP ARNTRHSLLG QDHRENDSLL
     MDWANMQQDA SFEQAPWSDL LIWALLLNRA QMAIYFWEKG SNSVASALGA CLLLRVMARL
     EWEAEEAARR KDLAAKFESM SVDLFGECYH NSEYRAARLL LRRCPLWGEA TCLQLAMQAD
     ARAFFAQDGV QSLLTQKWWG EMDSTNPIWA LLLTFFCPPL IYTNLILFRK SEEEPTQKDL
     DFDMDSSMNG AGPLGPAEPS AKVALERRRR RRPGHTLCCG GCSKRWSYFW GAPVTAFLGN
     VVSYLLFLLL FAHVLLVDFQ PTKPGVFELL LYFWAFTLLC EELRQGLGGG WGTLANGGPG
     PGKAPLRHRL HLYLLDTWNQ CDLLALTCFL LGVGCRLTPG LFDLGRTVLC LDFMIFTLRL
     LHIFTVNKQL GPKIVIVSKM MKDVFFFLFF LCVWLVAYGV ATEGILRPQD RSLPSILRRV
     FYRPYLQIFG QIPQEEMDVA LMNPSNCSAE RGSWAHPEGP VAGSCVSQYA NWLVVLLLIV
     FLLVANILLL NLLIAMFSYT FNKVHGNSDL YWKAQRYSLI REFHSRPALA PPLIIISHLR
     LLFKWLRRCH RTNLPASPVF EHFRVCLSKE AERTLLTWES VHKENFLLAQ ARDKRDSDSE
     RLKRTSQKVD TALKQLGQIR EYDRRLRGLE REVQHCSRVL TWMAEALSHS ALLPPGGPPP
     PSPTGSKD
//