SCY2B_ARATH
ID SCY2B_ARATH Reviewed; 909 AA.
AC Q9C9H8; Q0WM08;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=SCY1-like protein 2 B {ECO:0000303|PubMed:28751315};
DE AltName: Full=Inactive protein kinase SCYL2B {ECO:0000305};
GN Name=SCYL2B {ECO:0000303|PubMed:28751315};
GN OrderedLocusNames=At1g71410 {ECO:0000312|Araport:AT1G71410};
GN ORFNames=F26A9.21 {ECO:0000312|EMBL:AAG51833.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH VTI11; VTI12 AND CHC1,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, 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). Essential for polarized
CC root hair development probably by mediating the root hair tip
CC localization of cellulose synthase-like D3 (CSLD3) (PubMed:28751315).
CC {ECO:0000269|PubMed:28751315}.
CC -!- SUBUNIT: Interacts with VTI11, VTI12 and CHC1.
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: Expressed in shoot and root vascular tissues
CC (PubMed:28751315). In root cap regions, accumulates in columella cells
CC and lateral root caps (PubMed:28751315). Also observed specialized cell
CC types such as trichomes, guard cells and root hairs (PubMed:28751315).
CC {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: Abnormal root hair development (e.g. shorter with
CC abnormal shapes) (PubMed:28751315). The double mutant scyl2a scyl2b has
CC short root hairs and small shoots (PubMed:28751315).
CC {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}.
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DR EMBL; AC016163; AAG51833.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35198.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60464.1; -; Genomic_DNA.
DR EMBL; AK221244; BAD93866.1; -; mRNA.
DR EMBL; AK230027; BAF01849.1; -; mRNA.
DR RefSeq; NP_001322749.1; NM_001334498.1.
DR RefSeq; NP_177297.1; NM_105810.4.
DR AlphaFoldDB; Q9C9H8; -.
DR SMR; Q9C9H8; -.
DR IntAct; Q9C9H8; 1.
DR STRING; 3702.AT1G71410.1; -.
DR PaxDb; Q9C9H8; -.
DR PRIDE; Q9C9H8; -.
DR ProteomicsDB; 175225; -.
DR EnsemblPlants; AT1G71410.1; AT1G71410.1; AT1G71410.
DR EnsemblPlants; AT1G71410.2; AT1G71410.2; AT1G71410.
DR GeneID; 843482; -.
DR Gramene; AT1G71410.1; AT1G71410.1; AT1G71410.
DR Gramene; AT1G71410.2; AT1G71410.2; AT1G71410.
DR KEGG; ath:AT1G71410; -.
DR Araport; AT1G71410; -.
DR TAIR; locus:2825374; AT1G71410.
DR eggNOG; KOG2137; Eukaryota.
DR HOGENOM; CLU_008724_4_0_1; -.
DR InParanoid; Q9C9H8; -.
DR OMA; MAHKCIP; -.
DR OrthoDB; 196028at2759; -.
DR PhylomeDB; Q9C9H8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9H8; 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:0035619; C:root hair tip; IDA:TAIR.
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 GO; GO:0080147; P:root hair cell development; IMP:UniProtKB.
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..909
FT /note="SCY1-like protein 2 B"
FT /id="PRO_0000454398"
FT DOMAIN 39..343
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 311..348
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 350..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 624..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 204
FT /note="T -> I (in Ref. 3; BAF01849)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 909 AA; 98764 MW; 9EB448EEFCDA94F4 CRC64;
MSINMKTFTQ ALARTAAVIE KTVHTTVQEV TGPKALQDYE LLDQIGSAGP GLAWKLYAAK
ARDSTRPQQY PTVCVWMLDK RALSEARVRA NLSKAAEDAF LDLIRADAGK LVRLRHPGVV
HVVQALDENK NAMALVTEPL FASVANALGN VENVGNVPKD LKSMEMSLLE VKHGLLQISE
TLNFLHNNAN LIHRAISPEN VLITSAGSWK LAGFGFAISA AQAGNLDNMQ SFHYSEYDVE
DSILPVQPSL NYTAPELMRS KSPSAGASSD IFSFGCLAYH LVARKPLFDC NNNVKMYMNT
LNYITNESFS SIPSELVSDL QRMLSTNESF RPTALDFTGS NFFRSDARLR ALRFLDHLLE
RDNMQKSEFL KALSDMWKDF DSRVLRYKVL PPLCAELRNL VLQPIILPMV LTIAQSQDRT
DFELITLPAL VPVLSTASGD TLLLLVKHAD LITNKTDSEH LVSHVLPLLL RAYNDNDVRI
QEEVLKRSTS VAKQLDGQVV RQAILPRVHG LALKTTVAAV RVNALLCLAE LVQTLDKPAA
IEILETIQRC TAVDRSAPTL MCTLAVANAI LKQYGVEFTA EHVLTLMMPL LTAQQLNVQQ
FAKYMLFVKD ILRKIEEKRG VTVNDSGVPE VKPHSAANGL QFQSSTQIPE KVASAAKSSP
AWDEDWGSPS KDSAVGNPAS SRHNTNDQFN KSTDQSQPSI MSTLPNKTTA PTTCPAVDIE
WPPRQSSSLT APATDNQTQL NTGTSFASGF DELDPFANWP PRPNNGASVA STGLKNGAAS
NFSNNLPGGT HFQTANNDNW AFSSASLSSL KPPQQGNQGI SANNQDPLNS FGVPKQSQGM
PSFTSGSYNN QKPADISSIF GSSKTEPSAM KLAPPPSIAM GRGRGRGRGG TGTSTSKPSG
SQPSLLDLL
