AB1K1_ARATH
ID AB1K1_ARATH Reviewed; 682 AA.
AC Q8RWG1; O49588;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein ACTIVITY OF BC1 COMPLEX KINASE 1, chloroplastic {ECO:0000303|PubMed:23673981};
DE Short=ABC1-LIKE KINASE 1 {ECO:0000303|PubMed:23673981};
DE EC=2.7.-.- {ECO:0000255|PROSITE-ProRule:PRU00159};
DE EC=2.7.11.1 {ECO:0000269|PubMed:24267661};
DE AltName: Full=Protein ABC1-LIKE KINASE RELATED TO CHLOROPHYLL DEGRADATION AND OXIDATIVE STRESS 1 {ECO:0000303|PubMed:22447966};
DE Short=AtACDO1 {ECO:0000303|PubMed:22447966};
DE AltName: Full=Protein BLEACHING AND DWARF IN RED LIGHT 1 {ECO:0000303|PubMed:25882344};
DE AltName: Full=Protein PROTON GRADIENT REGULATION 6 {ECO:0000303|PubMed:24267661};
DE Flags: Precursor;
GN Name=ABC1K1 {ECO:0000303|PubMed:23673981};
GN Synonyms=ACDO1 {ECO:0000303|PubMed:22447966},
GN BDR1 {ECO:0000303|PubMed:25882344}, PGR6 {ECO:0000303|PubMed:24267661};
GN OrderedLocusNames=At4g31390 {ECO:0000312|Araport:AT4G31390};
GN ORFNames=F3L17.6 {ECO:0000312|EMBL:CAB79857.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=16461379; DOI=10.1104/pp.105.076083;
RA Ytterberg A.J., Peltier J.-B., van Wijk K.J.;
RT "Protein profiling of plastoglobules in chloroplasts and chromoplasts. A
RT surprising site for differential accumulation of metabolic enzymes.";
RL Plant Physiol. 140:984-997(2006).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION BY METHYL VIOLOGEN.
RC STRAIN=cv. Columbia;
RX PubMed=22447966; DOI=10.1093/jxb/ers072;
RA Yang S., Zeng X., Li T., Liu M., Zhang S., Gao S., Wang Y., Peng C., Li L.,
RA Yang C.;
RT "AtACDO1, an ABC1-like kinase gene, is involved in chlorophyll degradation
RT and the response to photooxidative stress in Arabidopsis.";
RL J. Exp. Bot. 63:3959-3973(2012).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=22274653; DOI=10.1104/pp.111.193144;
RA Lundquist P.K., Poliakov A., Bhuiyan N.H., Zybailov B., Sun Q.,
RA van Wijk K.J.;
RT "The functional network of the Arabidopsis plastoglobule proteome based on
RT quantitative proteomics and genome-wide coexpression analysis.";
RL Plant Physiol. 158:1172-1192(2012).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH ABC1K3.
RC STRAIN=cv. Columbia;
RX PubMed=23673981; DOI=10.1105/tpc.113.111120;
RA Lundquist P.K., Poliakov A., Giacomelli L., Friso G., Appel M.,
RA McQuinn R.P., Krasnoff S.B., Rowland E., Ponnala L., Sun Q., van Wijk K.J.;
RT "Loss of plastoglobule kinases ABC1K1 and ABC1K3 causes conditional
RT degreening, modified prenyl-lipids, and recruitment of the jasmonic acid
RT pathway.";
RL Plant Cell 25:1818-1839(2013).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=24267661; DOI=10.1111/tpj.12385;
RA Martinis J., Glauser G., Valimareanu S., Stettler M., Zeeman S.C.,
RA Yamamoto H., Shikanai T., Kessler F.;
RT "ABC1K1/PGR6 kinase: a regulatory link between photosynthetic activity and
RT chloroplast metabolism.";
RL Plant J. 77:269-283(2014).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=25882344; DOI=10.1016/j.molp.2015.04.003;
RA Huang H., Yang M., Su Y., Qu L., Deng X.W.;
RT "Arabidopsis atypical kinases ABC1K1 and ABC1K3 act oppositely to cope with
RT photodamage under red light.";
RL Mol. Plant 8:1122-1124(2015).
CC -!- FUNCTION: Kinase that can phosphorylate the tocopherol cyclase VTE1, a
CC key enzyme of tocopherol (vitamin E) metabolism and involved in the
CC recycling of oxidated alpha-tocopherol quinone, possibly stabilizing it
CC at plastoglobules. Regulates also plastoglobule protein composition
CC (PubMed:24267661). Prevents photodamage of chloroplasts under
CC continuous red light, thus working in opposition to ABC1K3
CC (PubMed:25882344). Together with ABC1K1, contributes to plastoglobule
CC (PG) function in prenyl-lipid metabolism, stress response, and
CC thylakoid remodeling (PubMed:23673981, PubMed:24267661). Involved in
CC chlorophyll degradation and in the maintenance of the number of
CC chlorophyll-binding photosynthetic thylakoid membranes
CC (PubMed:22447966). Ensures photosynthetic electron transport by
CC regulating the homeostasis of plastoquinone, beta-carotene and
CC xanthophyll lutein, as well as membrane antioxidant tocopherol
CC metabolism (PubMed:24267661). Seems to affect specifically stability or
CC turnover of D1 protein, product of psbA, one of the four core subunits
CC of the photosystem II (PSII) (PubMed:25882344). Required for
CC photooxidative stress responses, including the induction of oxidative
CC stress response genes (e.g. FSD1, CSD1, CAT1, and UTG71C1), to prevent
CC photosystem II core and chlorophyll degradations (PubMed:22447966,
CC PubMed:23673981, PubMed:24267661). {ECO:0000269|PubMed:22447966,
CC ECO:0000269|PubMed:23673981, ECO:0000269|PubMed:24267661,
CC ECO:0000269|PubMed:25882344}.
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 Evidence={ECO:0000269|PubMed:24267661};
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; Evidence={ECO:0000269|PubMed:24267661};
CC -!- SUBUNIT: Interacts with ABC1K3 in plastoglobules (PG).
CC {ECO:0000269|PubMed:23673981}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast, plastoglobule
CC {ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:22274653}. Plastid,
CC chloroplast {ECO:0000269|PubMed:22447966}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8RWG1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RWG1-2; Sequence=VSP_025072;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues (e.g. especially in
CC leaves) at all developmental stages from seed germination to flowering,
CC except in the root tips. {ECO:0000269|PubMed:22447966}.
CC -!- INDUCTION: Up-regulated by methyl viologen (paraquat, MV) treatment, a
CC herbicide triggering photooxidative stress.
CC {ECO:0000269|PubMed:22447966}.
CC -!- DISRUPTION PHENOTYPE: High chlorophyll fluorescence and reduced non-
CC photochemical quenching (NPQ) caused by defects in photosynthetic
CC electron transport. Specifically deficient in the electron carrier
CC plastoquinone, as well as in beta-carotene and the xanthophyll lutein,
CC and defective in membrane antioxidant tocopherol metabolism. Altered
CC plastoglobule protein composition (PubMed:24267661). Abnormal
CC development with albino cotyledons and paler mesophyll cells leading to
CC yellow-green leaves due to reduced contents of carotenoids and
CC chlorophyll, as well as changes in the numbers of chlorophyll-binding
CC proteins of the photosynthetic complexes (PubMed:22447966,
CC PubMed:24267661, PubMed:25882344). In bdr1-1 and bdr1-2, increased
CC accumulation of anthocyanin under red and blue light conditions.
CC Exposure to red light for 5 days leads to dwarf plants with pale green
CC rosette leaves. Reduced level of D1 protein, product of psbA, one of
CC the four core subunits of the photosystem II (PSII) (PubMed:25882344).
CC Increased levels of chlorophyll degradation products such as
CC chlorophyllide (Chlide) a and pheophorbide a. Stronger photosynthetic
CC and metabolic perturbations in response to high light stress and methyl
CC viologen (paraquat, MV), a herbicide triggering photooxidative stress,
CC strongly affecting carbohydrate metabolism (PubMed:22447966,
CC PubMed:24267661). However, the mutant acclimates to high light after 7
CC days together with a recovery of carotenoid levels and a drastic
CC alteration in the starch-to-sucrose ratio (PubMed:24267661). Lower
CC transcript levels of the oxidative stress response genes FSD1, CSD1,
CC CAT1, and UTG71C1 after MV treatment (PubMed:22447966). Conditional
CC light stress phenotype in the double mutant abc1k1 abc1k3 that displays
CC rapid chlorosis upon high light stress and slower, but irreversible,
CC senescence-like phenotype during moderate light stress, drought or
CC nitrogen limitation, but not cold stress. This senescence-like
CC phenotype is associated with the degradation of the photosystem II core
CC and up-regulation of chlorophyll degradation. Modified prenyl-lipid
CC composition in plastoglobules (PG) probably due to reduced VTE1
CC activity and loss of CCD4. Abnormal recruitment of plastid jasmonate
CC biosynthesis enzymes in PG (PubMed:23673981).
CC {ECO:0000269|PubMed:22447966, ECO:0000269|PubMed:23673981,
CC ECO:0000269|PubMed:24267661, ECO:0000269|PubMed:25882344}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16542.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79857.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021633; CAA16542.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161578; CAB79857.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85903.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85904.1; -; Genomic_DNA.
DR EMBL; AY093113; AAM13112.1; -; mRNA.
DR EMBL; BT008424; AAP37783.1; -; mRNA.
DR PIR; T04506; T04506.
DR RefSeq; NP_001031763.1; NM_001036686.1. [Q8RWG1-2]
DR RefSeq; NP_194867.2; NM_119288.3. [Q8RWG1-1]
DR AlphaFoldDB; Q8RWG1; -.
DR SMR; Q8RWG1; -.
DR STRING; 3702.AT4G31390.1; -.
DR PaxDb; Q8RWG1; -.
DR PRIDE; Q8RWG1; -.
DR ProteomicsDB; 243298; -. [Q8RWG1-1]
DR EnsemblPlants; AT4G31390.1; AT4G31390.1; AT4G31390. [Q8RWG1-1]
DR EnsemblPlants; AT4G31390.2; AT4G31390.2; AT4G31390. [Q8RWG1-2]
DR GeneID; 829266; -.
DR Gramene; AT4G31390.1; AT4G31390.1; AT4G31390. [Q8RWG1-1]
DR Gramene; AT4G31390.2; AT4G31390.2; AT4G31390. [Q8RWG1-2]
DR KEGG; ath:AT4G31390; -.
DR Araport; AT4G31390; -.
DR TAIR; locus:2128116; AT4G31390.
DR eggNOG; KOG1235; Eukaryota.
DR HOGENOM; CLU_006533_4_2_1; -.
DR InParanoid; Q8RWG1; -.
DR PhylomeDB; Q8RWG1; -.
DR PRO; PR:Q8RWG1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8RWG1; baseline and differential.
DR Genevisible; Q8RWG1; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0010287; C:plastoglobule; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IMP:UniProtKB.
DR GO; GO:0015996; P:chlorophyll catabolic process; IMP:TAIR.
DR GO; GO:0009767; P:photosynthetic electron transport chain; IMP:UniProtKB.
DR GO; GO:0080177; P:plastoglobule organization; IMP:UniProtKB.
DR GO; GO:1904143; P:positive regulation of carotenoid biosynthetic process; IMP:UniProtKB.
DR GO; GO:1902326; P:positive regulation of chlorophyll biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0031540; P:regulation of anthocyanin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010109; P:regulation of photosynthesis; IMP:UniProtKB.
DR GO; GO:1902171; P:regulation of tocopherol cyclase activity; IDA:UniProtKB.
DR GO; GO:0009637; P:response to blue light; IMP:UniProtKB.
DR GO; GO:1901562; P:response to paraquat; IEP:UniProtKB.
DR GO; GO:0080183; P:response to photooxidative stress; IMP:UniProtKB.
DR GO; GO:0010114; P:response to red light; IMP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
DR GO; GO:0010027; P:thylakoid membrane organization; IMP:UniProtKB.
DR InterPro; IPR004147; ABC1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF03109; ABC1; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chloroplast; Kinase; Nucleotide-binding;
KW Plastid; Reference proteome; Stress response; Transferase; Transit peptide.
FT TRANSIT 1..79
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 80..682
FT /note="Protein ACTIVITY OF BC1 COMPLEX KINASE 1,
FT chloroplastic"
FT /id="PRO_0000286524"
FT DOMAIN 236..567
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 400
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 242..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 321..345
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_025072"
SQ SEQUENCE 682 AA; 76757 MW; E31B0AC7C7812F38 CRC64;
MESIHCNSLL NPNFSLNQRR RRINHAVLNR RDALLRSLNA VELRRSRTFS AVRTSNFSVT
AAATDVGGRN STDASVMTTA MSGVERGVRV GKSSSALEQL DIERGVCVPF RKYSPETVRS
KVLESRGAVV SLVSRGVEIV WTLGLYWSTL TYDFLVGRDE EVVPFRARQL RNLLCNLGPS
FIKAGQVLAN RPDIIREDYM NELCILQDDV PPFPNEVAFN IIEEELGQPL ENIFSKISSQ
TIAAASLGQV YRATLRATGE DVAIKVQRPQ IEPIIYRDLF LFRTLASFLN GFSLQKLGCN
AELIVDEFGE KLLEELDYTL EARNIEDFLE NFKDDPTVKI PGVYKNLCGP RVLVMEWIDG
IRCTDPQAIK DAGIDLNGFL TVGVSAALRQ LLEFGLFHGD PHPGNIFAMQ DGRIAYVDFG
NVAVLSQQNK QILIDAVVHA VNEDYGEMAN DFTRLGFLAK DTDVSPIVPA LEAIWQNSAG
KGLADFNFRS VTGQFNKLVY DFPIRIPERF SLVIRSLLTQ EGICFTLKPD FKFLEVAYPY
VAKRLLTDPN PALRERLIQV LFKDGVFQWK RLENLLSLAK ENVAKMSSNP NLRVKRVESK
LDLTDTIKDG ARLFLLDEGI RRKLILALTE DSKLHVEELV DVYRLVEDEV DIPTLAMQVV
QDLPNVFRDF VLSWSNSVLS DR
