PKP4_MOUSE
ID PKP4_MOUSE Reviewed; 1190 AA.
AC Q68FH0; A2AS46; Q640N0; Q68G56; Q8BK47; Q8BVH1; Q9CRE3;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Plakophilin-4;
DE AltName: Full=Armadillo-related protein;
GN Name=Pkp4; Synonyms=Armrp;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, Eye, and Mammary cancer;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 747-1190 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb, Ovary, and Uterus;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313; SER-405 AND SER-1133,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-371 AND TYR-477, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-84; SER-132; SER-136;
RP SER-139; SER-220; SER-230; SER-280; SER-313; SER-326; SER-336; SER-402;
RP SER-405; THR-411; SER-421; SER-426; SER-437; SER-509; SER-511; SER-514;
RP SER-775; THR-1012; THR-1016; SER-1044; SER-1090; SER-1099 AND SER-1133, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-253 AND ARG-269, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Plays a role as a regulator of Rho activity during
CC cytokinesis. May play a role in junctional plaques (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via the C-terminus) with FRMPD2 (via the PDZ 2
CC domain). Interacts with PDZD2. Interacts with RHOA; the interaction is
CC detected at the midbody. Interacts with ECT2; the interaction is
CC detected at the midbody (By similarity). Interacts with CCDC85B (By
CC similarity). {ECO:0000250|UniProtKB:Q99569}.
CC -!- SUBCELLULAR LOCATION: Cell junction, desmosome {ECO:0000250}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000250}. Midbody {ECO:0000250}. Cell
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Note=Associated with the pericentrosomal region in interphase and with
CC spindle poles during mitosis. In anaphase, during chromosome
CC segregation, is recruited to the central microtubule bundle, focussed
CC at the spindle midzone and ultimately localizes to the midbody at
CC cytokinesis. Constituent of the midbody cytoskeletal matrix.
CC Colocalized with desmoplakin at desmosomal junctional plaques in
CC cultured epithelial cells (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q68FH0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68FH0-2; Sequence=VSP_012377;
CC Name=3;
CC IsoId=Q68FH0-3; Sequence=VSP_012374, VSP_012375, VSP_012376;
CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37187.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; AL845536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC078638; AAH78638.1; -; mRNA.
DR EMBL; BC079848; AAH79848.1; -; mRNA.
DR EMBL; BC082578; AAH82578.1; -; mRNA.
DR EMBL; AK021168; BAB32313.1; -; mRNA.
DR EMBL; AK077250; BAC36708.1; -; mRNA.
DR EMBL; AK078240; BAC37187.1; ALT_INIT; mRNA.
DR CCDS; CCDS16052.1; -. [Q68FH0-1]
DR CCDS; CCDS50588.1; -. [Q68FH0-2]
DR RefSeq; NP_080637.1; NM_026361.2. [Q68FH0-1]
DR RefSeq; NP_780673.2; NM_175464.2. [Q68FH0-2]
DR RefSeq; XP_006499234.1; XM_006499171.3. [Q68FH0-1]
DR AlphaFoldDB; Q68FH0; -.
DR SMR; Q68FH0; -.
DR BioGRID; 230696; 15.
DR IntAct; Q68FH0; 4.
DR MINT; Q68FH0; -.
DR STRING; 10090.ENSMUSP00000099815; -.
DR iPTMnet; Q68FH0; -.
DR PhosphoSitePlus; Q68FH0; -.
DR SwissPalm; Q68FH0; -.
DR MaxQB; Q68FH0; -.
DR PaxDb; Q68FH0; -.
DR PeptideAtlas; Q68FH0; -.
DR PRIDE; Q68FH0; -.
DR ProteomicsDB; 289517; -. [Q68FH0-1]
DR ProteomicsDB; 289518; -. [Q68FH0-2]
DR ProteomicsDB; 289519; -. [Q68FH0-3]
DR Antibodypedia; 33712; 183 antibodies from 29 providers.
DR DNASU; 227937; -.
DR Ensembl; ENSMUST00000102754; ENSMUSP00000099815; ENSMUSG00000026991. [Q68FH0-1]
DR Ensembl; ENSMUST00000168631; ENSMUSP00000129836; ENSMUSG00000026991. [Q68FH0-2]
DR GeneID; 227937; -.
DR KEGG; mmu:227937; -.
DR UCSC; uc008jtb.1; mouse. [Q68FH0-1]
DR UCSC; uc008jtd.1; mouse. [Q68FH0-2]
DR UCSC; uc008jtg.1; mouse. [Q68FH0-3]
DR CTD; 8502; -.
DR MGI; MGI:109281; Pkp4.
DR VEuPathDB; HostDB:ENSMUSG00000026991; -.
DR eggNOG; KOG1048; Eukaryota.
DR GeneTree; ENSGT00940000155773; -.
DR HOGENOM; CLU_007897_0_0_1; -.
DR InParanoid; Q68FH0; -.
DR OMA; KIEVCRL; -.
DR OrthoDB; 233858at2759; -.
DR PhylomeDB; Q68FH0; -.
DR TreeFam; TF321877; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 227937; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Pkp4; mouse.
DR PRO; PR:Q68FH0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q68FH0; protein.
DR Bgee; ENSMUSG00000026991; Expressed in ciliary body and 255 other tissues.
DR ExpressionAtlas; Q68FH0; baseline and differential.
DR Genevisible; Q68FH0; MM.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0044291; C:cell-cell contact zone; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0030057; C:desmosome; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IMP:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR028443; Plakophilin-4.
DR InterPro; IPR028435; Plakophilin/d_Catenin.
DR PANTHER; PTHR10372; PTHR10372; 1.
DR PANTHER; PTHR10372:SF8; PTHR10372:SF8; 1.
DR Pfam; PF00514; Arm; 3.
DR SMART; SM00185; ARM; 7.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
KW Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Methylation;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1190
FT /note="Plakophilin-4"
FT /id="PRO_0000064290"
FT REPEAT 517..556
FT /note="ARM 1"
FT REPEAT 559..598
FT /note="ARM 2"
FT REPEAT 603..643
FT /note="ARM 3"
FT REPEAT 861..900
FT /note="ARM 4"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 36..63
FT /evidence="ECO:0000255"
FT COMPBIAS 10..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99569"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99569"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99569"
FT MOD_RES 253
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 269
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99569"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 371
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99569"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 411
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 414
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99569"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 477
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1012
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1016
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1090
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1099
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..341
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012374"
FT VAR_SEQ 637
FT /note="V -> G (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012375"
FT VAR_SEQ 638..1190
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012376"
FT VAR_SEQ 1042..1084
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012377"
FT CONFLICT 328
FT /note="S -> F (in Ref. 2; AAH78638)"
FT /evidence="ECO:0000305"
FT CONFLICT 877
FT /note="V -> A (in Ref. 3; BAC36708)"
FT /evidence="ECO:0000305"
FT CONFLICT 1118
FT /note="D -> G (in Ref. 3; BAC36708)"
FT /evidence="ECO:0000305"
FT CONFLICT 1161
FT /note="K -> R (in Ref. 3; BAB32313)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1190 AA; 131551 MW; DB6548B5EBE72CFE CRC64;
MPAPEQGSLV EEGQPQTHQE AVSTGPGMEP ETTATTILAS VKEQELQFQR LTRELEVERQ
IVASQLERCR LGAESPSIAS TSSTEKSFPW RSTDVPNPGV SKPRVSDTIH PNNYLIRTEP
EQGTLYSPEQ TSLHESEGSL GNSRSSTQMN SYSDSGYQEA GSFHNSQTVN KADSRQHPFT
GSTSNHVVRT SRAEGQTLVQ PSVANRAMRR VSSVPSRAQS PSYVTSTGVS PSRGSLRTSL
GSGFGSPSVT DSRPLNPSAY SSSTLPAQRA ASPYSQRPAS PTAVRRVGSV TSRQTSNPNG
PVPQYQTTTR VGSPLTLTDA QTRVASPSQG QVGSSSPKRS GMTAVPQHLG PSLQRTVHDM
DQFGQQQYDI YERMVPPRPD SLTGLRSSYA SQHSQLGQEL RSAVSPDLHI TPIYEGRTYY
SPVYRSPNHG TVELQGSQTA LYRTGSVGIG NLQRTSSQRS TLTYQRNNYA LNTAATYAEP
YRPVQYRVQE CSYNRLQHTG PADDGATRSP SIDSIQKDPR EFAWRDPELP EVIHMLQHQF
PSVQANAAAY LQHLCFGDNK VKMEVYRLGG IKHLVDLLDH RVLEVQKNAC GALRNLVFGK
STDENKIAMK NVGGIPALLR LLRKSIDAEV RELVTGVLWN LSSCDAVKMT IIRDALSTLT
NTVIVPHSGW NNSSFDDDHK IKFQTSLVLR NTTGCLRNLS SAGEEARKQM RSCEGLVDSL
LYVIHTCVNT SDYDSKTVEN CVCTLRNLSY RLELEVPQAR LLGLNELDDL LGKESPSKDS
EPSCWGKKKK KKKRTPQEDQ WDGVGPIPGL SKSPKGVEML WHPSVVKPYL TLLAESSNPA
TLEGSAGSLQ NLSAGNWKFA AYIRAAVRKE KGLPILVELL RMDNDRVVSS VATALRNMAL
DVRNKELIGK YAMRDLVNRL PGGNGPSILS DETVAAICCA LHEVTSKNME NAKALADSGG
IEKLVNITKG RGDRSSLKVV KAAAQVLNTL WQYRDLRSIY KKDGWNQNHF ITPVSTLERD
RFKSHPSLST TNQQMSPIIQ SVGSTSSSPA LLGIREPRSE YDRTQPPMQY YNSQGDTTHK
GLYPGSSKPS PIYISSYSSP AREQNRRLQH QQLYYQDDST RKTLDAYRLY LQSPRSYEDP
YCDDRVHFPA STDYSTQYGL KSTTNYVDFY STKRPSYRAE QYPGSPDSWV
