SCY2A_ARATH
ID SCY2A_ARATH Reviewed; 913 AA.
AC F4I313; O23135;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=SCY1-like protein 2 A {ECO:0000303|PubMed:28751315};
DE AltName: Full=Inactive protein kinase SCYL2A {ECO:0000305};
GN Name=SCYL2A {ECO:0000303|PubMed:28751315};
GN OrderedLocusNames=At1g22870 {ECO:0000312|Araport:AT1G22870};
GN ORFNames=F19G10.17 {ECO:0000312|EMBL:AAB72172.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=28751315; DOI=10.1104/pp.17.00824;
RA Jung J.-Y., Lee D.W., Ryu S.B., Hwang I., Schachtman D.P.;
RT "SCYL2 genes are involved in clathrin-mediated vesicle trafficking and
RT essential for plant growth.";
RL Plant Physiol. 175:194-209(2017).
CC -!- FUNCTION: Probably inactive kinase (PubMed:28751315). Component of the
CC AP2-containing clathrin coat that regulates clathrin-dependent
CC trafficking at plasma membrane, TGN and endosomal system
CC (PubMed:28751315). Together with SCYL2B, required for cell growth,
CC plant growth and development (PubMed:28751315).
CC {ECO:0000269|PubMed:28751315}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:28751315}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000269|PubMed:28751315}. Prevacuolar compartment
CC membrane {ECO:0000269|PubMed:28751315}. Note=Colocalizes with the
CC clathrin heavy chain 1 (CHC1). {ECO:0000269|PubMed:28751315}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, seedlings, leaves, stems,
CC flowers, and, at low levels, in siliques.
CC {ECO:0000269|PubMed:28751315}.
CC -!- DEVELOPMENTAL STAGE: Mainly expressed in leaf mesophyll cells, and, at
CC low levels, in root vascular tissues. {ECO:0000269|PubMed:28751315}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- DISRUPTION PHENOTYPE: The double mutant scyl2a scyl2b has short root
CC hairs and small shoots. {ECO:0000269|PubMed:28751315}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the kinase superfamily, lacks the
CC residues involved in ATP binding, suggesting that it has no protein
CC kinase activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB72172.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF000657; AAB72172.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30298.1; -; Genomic_DNA.
DR PIR; F86362; F86362.
DR RefSeq; NP_173700.2; NM_102133.3.
DR AlphaFoldDB; F4I313; -.
DR SMR; F4I313; -.
DR STRING; 3702.AT1G22870.1; -.
DR PaxDb; F4I313; -.
DR PRIDE; F4I313; -.
DR ProteomicsDB; 218070; -.
DR EnsemblPlants; AT1G22870.1; AT1G22870.1; AT1G22870.
DR GeneID; 838892; -.
DR Gramene; AT1G22870.1; AT1G22870.1; AT1G22870.
DR Araport; AT1G22870; -.
DR TAIR; locus:2017784; AT1G22870.
DR eggNOG; KOG2137; Eukaryota.
DR HOGENOM; CLU_008724_4_0_1; -.
DR InParanoid; F4I313; -.
DR OrthoDB; 196028at2759; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I313; baseline and differential.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0032050; F:clathrin heavy chain binding; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Membrane; Reference proteome; Repeat.
FT CHAIN 1..913
FT /note="SCY1-like protein 2 A"
FT /id="PRO_0000454397"
FT DOMAIN 39..343
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 311..346
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 347..382
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 383..401
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 402..439
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 465..502
FT /note="HEAT 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00103"
FT REPEAT 499..537
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 578..617
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REGION 651..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 913 AA; 100056 MW; 237DEC89C0C366D1 CRC64;
MSINMRTLTQ ALAKTAAVIE KTVQTTVQEV TGPKPLQDYE LLDQIGSGGP GLAWKLYSAK
ARDSTRPQQY PTVCVWVLDK RALSEARARA GLSKAAEDAF LDLIRADSGK LVRLRHPGVV
HVVQALDENK NAMAMVTEPL FASVANALGN VENVDNVPKD LKSMEMSLLE VKHGLLQIAE
TLNFLHNNAH LIHRAVSPEN VFITSAGSWK LAGFGFAISQ AQDGNLDNLQ SFHYSEYDVE
DSILPLQPSL NYTAPELVRS KTSSAGVSSD IFSFGCLTYH LVARKPLFDC HNNVKMYMNT
LNYLTNETFS SIPSDLVSDL QRMLSMNESY RPTALDFTGS SFFRSDTRLR ALRFLDHMLE
RDNMQKSEFL KALSDMWKDF DSRVLRYKVL PPLCAELRNL VMQPVILPMV LTIAESQDKN
DFELTTLPAL VPVLSTATGD TLLLLIKRAE LIINKTNAEH LVSHVLPLLL RAYNDNDVRI
QEEVLKRSTS VAKQLDGQVV RQAILPRVHG LALKTTVAAV RVNALLCLAE LVQTLDKLAV
TEILQTIQRC TAVDRSAPTL MCTLAIANAI LKQYGVEFTS EHVLPLIIPL LTAQQLNVQQ
FAKYILFVKD ILRKIEEKRG VTVNDSGVPE VKPGCVADGL QFQTPTKKTE KVASAAKNSP
AWDEDWALPT KISAPRDPGP ANSPQFNNST VQSQSSNRTS VPTTCPAVDL EWPPRQSFNA
TAQPANDETR INAAGTPTTP SFDELDPFAN WPPRPNSAST ASGGFHNSTT TQPPINNSGS
GLRNNLTDGR QFQTTNNDFW AFGNASLSSM KSQQETSGIR ASNADPLTSF GIQNQNQGMP
SFGSSSYGNQ KPQADISSIF SSSRTEQSAM KLAPPPSIAV GRGRGRGRSG TSISKPNGSK
QQQTEQPSLL DLL
