MRCKA_MOUSE
ID MRCKA_MOUSE Reviewed; 1719 AA.
AC Q3UU96; B2RY49; Q4V9U7; Q6ZQA9; Q8R495;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Serine/threonine-protein kinase MRCK alpha;
DE EC=2.7.11.1;
DE AltName: Full=CDC42-binding protein kinase alpha;
GN Name=Cdc42bpa; Synonyms=Kiaa0451;
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] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1451-1719.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
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] OF 1-752 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 736-1006.
RA Behrend E.N., Kemppainen R.J.;
RT "MRCK-alpha interacts with Dexras1.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1376-1719.
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, and Pancreas;
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 [7]
RP FUNCTION, INTERACTION WITH FAM89B AND LIMK1, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=25107909; DOI=10.1074/jbc.m114.588079;
RA Lee I.C., Leung T., Tan I.;
RT "Adaptor protein LRAP25 mediates myotonic dystrophy kinase-related Cdc42-
RT binding kinase (MRCK) regulation of LIMK1 protein in lamellipodial F-actin
RT dynamics.";
RL J. Biol. Chem. 289:26989-27003(2014).
CC -!- FUNCTION: Serine/threonine-protein kinase which is an important
CC downstream effector of CDC42 and plays a role in the regulation of
CC cytoskeleton reorganization and cell migration. Regulates actin
CC cytoskeletal reorganization via phosphorylation of PPP1R12C and
CC MYL9/MLC2. In concert with MYO18A and LRP35A, is involved in modulating
CC lamellar actomyosin retrograde flow that is crucial to cell protrusion
CC and migration. Phosphorylates: PPP1R12A and LIMK2. May play a role in
CC TFRC-mediated iron uptake (By similarity). In concert with
CC FAM89B/LRAP25 mediates the targeting of LIMK1 to the lamellipodium
CC resulting in its activation and subsequent phosphorylation of CFL1
CC which is important for lamellipodial F-actin regulation
CC (PubMed:25107909). Triggers the formation of an extrusion apical actin
CC ring required for epithelial extrusion of apoptotic cells (By
CC similarity). {ECO:0000250|UniProtKB:Q5VT25,
CC ECO:0000269|PubMed:25107909}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Maintained in an inactive, closed conformation by
CC an interaction between the kinase domain and the negative
CC autoregulatory C-terminal coiled-coil region. Agonist binding to the
CC phorbol ester binding site disrupts this, releasing the kinase domain
CC to allow N-terminus-mediated dimerization and kinase activation by
CC transautophosphorylation. Inhibited by chelerythrine chloride (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer and homotetramer via the coiled coil regions.
CC Interacts tightly with GTP-bound but not GDP-bound CDC42. Forms a
CC tripartite complex with MYO18A and LRP35A with the latter acting as an
CC adapter connecting CDC42BPA and MYO18A. LRP35A binding results in
CC activation of CDC42BPA by abolition of its negative autoregulation.
CC Interacts with LURAP1 (By similarity). Interacts (via AGC-kinase C-
CC terminal domain) with FAM89B/LRAP25 (via LRR repeat). Forms a
CC tripartite complex with FAM89B/LRAP25 and LIMK1 (PubMed:25107909).
CC {ECO:0000250|UniProtKB:O54874, ECO:0000269|PubMed:25107909}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection,
CC lamellipodium {ECO:0000269|PubMed:25107909}. Note=Displays a dispersed
CC punctate distribution and concentrates along the cell periphery,
CC especially at the leading edge and cell-cell junction. This
CC concentration is PH-domain dependent (By similarity). Localizes in the
CC lamellipodium in a FAM89B/LRAP25-dependent manner (PubMed:25107909).
CC {ECO:0000250|UniProtKB:O54874, ECO:0000269|PubMed:25107909}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UU96-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UU96-2; Sequence=VSP_023679, VSP_023680;
CC -!- PTM: Proteolytically cleaved by caspases upon apoptosis induction. The
CC cleavage at Asp-478 by CASP3 increases its kinase activity (in vitro).
CC {ECO:0000250|UniProtKB:Q5VT25}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000305}.
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DR EMBL; AC125380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC096679; AAH96679.1; -; mRNA.
DR EMBL; BC158095; AAI58096.1; -; mRNA.
DR EMBL; AK138649; BAE23731.1; -; mRNA.
DR EMBL; AF492452; AAM10976.1; -; mRNA.
DR EMBL; AK129148; BAC97958.1; -; mRNA.
DR CCDS; CCDS83649.1; -. [Q3UU96-1]
DR RefSeq; NP_001333733.1; NM_001346804.1. [Q3UU96-1]
DR AlphaFoldDB; Q3UU96; -.
DR SMR; Q3UU96; -.
DR BioGRID; 230550; 4.
DR IntAct; Q3UU96; 2.
DR MINT; Q3UU96; -.
DR STRING; 10090.ENSMUSP00000106746; -.
DR iPTMnet; Q3UU96; -.
DR PhosphoSitePlus; Q3UU96; -.
DR EPD; Q3UU96; -.
DR jPOST; Q3UU96; -.
DR MaxQB; Q3UU96; -.
DR PaxDb; Q3UU96; -.
DR PeptideAtlas; Q3UU96; -.
DR PRIDE; Q3UU96; -.
DR ProteomicsDB; 290054; -. [Q3UU96-1]
DR ProteomicsDB; 290055; -. [Q3UU96-2]
DR Antibodypedia; 34655; 246 antibodies from 36 providers.
DR DNASU; 226751; -.
DR Ensembl; ENSMUST00000097450; ENSMUSP00000095059; ENSMUSG00000026490. [Q3UU96-1]
DR GeneID; 226751; -.
DR KEGG; mmu:226751; -.
DR UCSC; uc007dvu.2; mouse. [Q3UU96-1]
DR CTD; 8476; -.
DR MGI; MGI:2441841; Cdc42bpa.
DR VEuPathDB; HostDB:ENSMUSG00000026490; -.
DR eggNOG; KOG0612; Eukaryota.
DR GeneTree; ENSGT01030000234517; -.
DR InParanoid; Q3UU96; -.
DR OrthoDB; 759391at2759; -.
DR PhylomeDB; Q3UU96; -.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR BioGRID-ORCS; 226751; 0 hits in 77 CRISPR screens.
DR ChiTaRS; Cdc42bpa; mouse.
DR PRO; PR:Q3UU96; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3UU96; protein.
DR Bgee; ENSMUSG00000026490; Expressed in animal zygote and 228 other tissues.
DR ExpressionAtlas; Q3UU96; baseline and differential.
DR Genevisible; Q3UU96; MM.
DR GO; GO:0042641; C:actomyosin; ISO:MGI.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0031032; P:actomyosin structure organization; ISO:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; ISO:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR GO; GO:0007097; P:nuclear migration; IMP:MGI.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; ISO:MGI.
DR CDD; cd00029; C1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR031597; KELK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR026611; Ser/Thr_kinase_MRCK_alpha.
DR PANTHER; PTHR22988:SF31; PTHR22988:SF31; 2.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF08826; DMPK_coil; 1.
DR Pfam; PF15796; KELK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Coiled coil; Cytoplasm;
KW Kinase; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..1719
FT /note="Serine/threonine-protein kinase MRCK alpha"
FT /id="PRO_0000280455"
FT DOMAIN 77..343
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 344..414
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 1069..1188
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1214..1486
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT DOMAIN 1558..1571
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT ZN_FING 999..1049
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1579..1719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 437..670
FT /evidence="ECO:0000255"
FT COILED 713..820
FT /evidence="ECO:0000255"
FT COILED 880..943
FT /evidence="ECO:0000255"
FT COMPBIAS 1589..1663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1682..1719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 83..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 478..479
FT /note="Cleavage; by CASP3 in vitro"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 222
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 234
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 240
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 1532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 1598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 1600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 1616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 1638
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 1651
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 1656
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 1680
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 1706
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 1708
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023679"
FT VAR_SEQ 550..630
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023680"
FT CONFLICT 1451..1453
FT /note="VYS -> HEG (in Ref. 2; AAH96679)"
FT /evidence="ECO:0000305"
FT CONFLICT 1535
FT /note="V -> F (in Ref. 2; AAH96679)"
FT /evidence="ECO:0000305"
FT CONFLICT 1612
FT /note="G -> V (in Ref. 5; BAC97958)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1719 AA; 195536 MW; 362101C884240865 CRC64;
MSGEVRLRQL EQFILDGPAQ TNGQCFSVET LLDILICLYD ECNNSPLRRE KNILEYLEWA
KPFTSKVKQM RLHREDFEIL KVIGRGAFGE VAVVKLKNAD KVFAMKILNK WEMLKRAETA
CFREERDVLV NGDSKWITTL HYAFQDDNNL YLVMDYYVGG DLLTLLSKFE DRLPEEMARF
YLAEMVIAID SVHQLHYVHR DIKPDNILMD MNGHIRLADF GSCLKLMEDG TVQSSVAVGT
PDYISPEILQ AMEDGKGRYG PECDWWSLGV CMYEMLYGET PFYAESLVET YGKIMNHKER
FQFPAQVTDV SENAKDLIRR LICSREHRLG QNGIEDFKKH PFFSGIDWDN IRNCEAPYIP
EVSSPTDTSN FDVDDDCLKN SETMPPPTHT AFSGHHLPFV GFTYTSSCVL SDRSCLRVTA
GPTSLDLDVS VQRTLDNNLA TEAYERRIKR LEQEKLELTR KLQESTQTVQ ALQYSTVDGP
LTASKDLEIK SLKEEIEKLR KQVAEVNHLE QQLEEANSVR RELDDAFRQI KASEKQIKTL
QQEREELNKE LVQASERLKN QSKELKDAHC QRKLAMQEFM EINERLTELH TQKQKLARHV
RDKEEEVDLV MQKAESLRQE LRRAERAKKE LEVHTEALIA EASKDKKLRE QSEHYSKQLE
NELEGLKQKQ ISYSPGICSI EHQQEITKLK TDLEKKSIFY EEEISKREGI HASEIKNLKK
ELHDSEGQQL ALNKEILVLK DKLEKTRRES QSEREEFENE FKQQYEREKV LLTEENKKLT
SELDKLTSLY ESLSLRNQHL EEEVKDLADK KESVAHWEAQ ITEIIQWVSD EKDARGYLQA
LASKMTEELE ALRNSSLGTR ATDMPWKMRR FAKLDMSARL ELQSALDAEI RAKQAIQEEL
NKVKASNILT ECKLKDSEKK NLELLSEIEQ LIKDTEELRS EKGIEHQDSQ HSFLAFLNTP
TDALDQFEIA DCAPLPAHTP TLRKKGCPAS TGFPPKRKTH QFFVKSFTAP TKCHQCTSLM
VGLIRQGCSC EVCGFSCHIT CVNKAPTVCP VPPEQTKGPL GIDPQKGVGT AYEGHVRIPK
PAGVKKGWQR ALAVVCDFKL FLYDIAEGKA SQPTSVISQV IDMRDEEFSV SSVLASDVIH
ASRKDIPCIF RVTASQLSAP SNKCSILMLA DSENERSKWV GVLSELHKIL KKNKFRDRSV
YVPKEAYDST LPLIKTTQAA AIIDHERIAL GNEEGLFVVH VTKDEIVRVG DNKKIHQIEL
IPSDQLVAVI SGRNRHVRLF PMSALDGRET DFYKLAETKG CQTIAAGKVR HGALSCLCVA
MKRQVLCYEL FQSKTRHRKF KEIQVPCNVQ WMAIFSEHLC VGFQSGFLRY PLNGEGGPCN
MLHSNDHTLS FISHQPMDAL CAVEISNKEY LLCFNSIGIY TDCQGRRSRQ QELMWPANPS
SCCYNAPYLS VYSENAVDIF DVNSMEWIQT LPLKKVRPLN TEGSLNLLGL ETIRLIYFKN
KMAEGDELVV PETSDNSRKQ MVRNINNKRR YSFRVPEEER MQQRREMLRD PEMRNKLISN
PTNFNHIAHM GPGDGIQILK DLPMNPRPQE SRTVFSGSVS IPSITKSRPE PGRSMSASSG
LSARSSAQNG SALKREFSGG SYNTKRQPMP SPSEGSLSSG GMDQGSDAPA RDYDGEDSDS
PRHSTASNSS NLSSPPSPIS PQKTKSLSLE STDRGSWDP
