PSRK_ARATH
ID PSRK_ARATH Reviewed; 546 AA.
AC P0DH87; B0F2A9; B0F2B0; D6NTN9; D6NTP0; D6NTP1; D6NTP2; D6NTP6; D6NTP7;
AC D6NTP8; O81904;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Putative inactive G-type lectin S-receptor-like serine/threonine-protein kinase SRK;
DE AltName: Full=Pseudogene of S-locus receptor kinase A;
DE Flags: Precursor;
GN Name=PSEUDOSRKA; OrderedLocusNames=At4g21370; ORFNames=T6K22.100;
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 FUNCTION.
RX PubMed=15505209; DOI=10.1073/pnas.0406970101;
RA Nasrallah M.E., Liu P., Sherman-Broyles S., Boggs N.A., Nasrallah J.B.;
RT "Natural variation in expression of self-incompatibility in Arabidopsis
RT thaliana: implications for the evolution of selfing.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16070-16074(2004).
RN [4]
RP FUNCTION, AND REVIEW.
RX PubMed=17237349; DOI=10.1105/tpc.106.048199;
RA Sherman-Broyles S., Boggs N., Farkas A., Liu P., Vrebalov J.,
RA Nasrallah M.E., Nasrallah J.B.;
RT "S locus genes and the evolution of self-fertility in Arabidopsis
RT thaliana.";
RL Plant Cell 19:94-106(2007).
RN [5]
RP FUNCTION.
RX PubMed=17656687; DOI=10.1126/science.1143153;
RA Tang C., Toomajian C., Sherman-Broyles S., Plagnol V., Guo Y.-L., Hu T.T.,
RA Clark R.M., Nasrallah J.B., Weigel D., Nordborg M.;
RT "The evolution of selfing in Arabidopsis thaliana.";
RL Science 317:1070-1072(2007).
CC -!- FUNCTION: Truncated and inactivated form of SRK, the female specificity
CC determinant of self-incompatibility when active. Most A.thaliana
CC cultivars contain such an inactive form and thus, are self-fertiles.
CC {ECO:0000269|PubMed:15505209, ECO:0000269|PubMed:17237349,
CC ECO:0000269|PubMed:17656687}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. In strain cv. Columbia,
CC a frameshift mutation introduces a premature stop codon leading to a
CC truncated SRK protein. A complete sequence for SRK can be found in
CC strains cv. Pog-0 and cv. Wei-1 (AC P0DH86). {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA20202.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79136.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Do it yourself - Issue 128
CC of May 2011;
CC URL="https://web.expasy.org/spotlight/back_issues/128";
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DR EMBL; AL031187; CAA20202.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161554; CAB79136.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T05179; T05179.
DR AlphaFoldDB; P0DH87; -.
DR SMR; P0DH87; -.
DR PeptideAtlas; P0DH87; -.
DR PRIDE; P0DH87; -.
DR Araport; AT4G21370; -.
DR InParanoid; P0DH87; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P0DH87; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR CDD; cd00028; B_lectin; 1.
DR Gene3D; 2.90.10.10; -; 1.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR022126; S-locus_recpt_kinase.
DR InterPro; IPR000858; S_locus_glycoprot_dom.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF12398; DUF3660; 1.
DR Pfam; PF08276; PAN_2; 1.
DR Pfam; PF00954; S_locus_glycop; 1.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00473; PAN_AP; 1.
DR SUPFAM; SSF51110; SSF51110; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
DR PROSITE; PS50948; PAN; 1.
PE 5: Uncertain;
KW ATP-binding; Cell membrane; Disulfide bond; Glycoprotein; Lectin; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..546
FT /note="Putative inactive G-type lectin S-receptor-like
FT serine/threonine-protein kinase SRK"
FT /id="PRO_0000413168"
FT TOPO_DOM 32..441
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..546
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..154
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 293..329
FT /note="EGF-like; atypical"
FT DOMAIN 348..428
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 524..546
FT /note="Protein kinase"
FT BINDING 530..538
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 297..309
FT /evidence="ECO:0000250"
FT DISULFID 303..317
FT /evidence="ECO:0000250"
FT DISULFID 378..403
FT /evidence="ECO:0000250"
FT DISULFID 382..388
FT /evidence="ECO:0000250"
SQ SEQUENCE 546 AA; 62093 MW; 7815DBBCAD3878BA CRC64;
MRGELPNKHH SYTFFVFLFF FLILFPDLSI SVNTLSATES LTISSNKTIV SPGGVFELGF
FRILGDSWYL GIWYKKISQR TYVWVANRDT PLSNPIGILK ISNANLVILD NSDTHVWSTN
LTGAVRSSVV AELLDNGNFV LRGSKINESD EFLWQSFDFP TDTLLPQMKL GRDHKRGLNR
FVTSWKSSFD PSSGSFMFKL ETLGLPEFFG FTSFLEVYRS GPWDGLRFSG ILEMQQWDDI
IYNFTENREE VAYTFRVTDH NSYSRLTINT VGRLEGFTWE PTQQEWNMFW FMPKDTCDLY
GICGPYAYCD MSTSPTCNCI KGFQPLSPQD WASGDVTGRC RRKTQLTCGE DRFFRLMNMK
IPATTAAIVD KRIGLKECEE KCKTHCNCTA YANSDIRNGG SGCIIWIGEF RDIRNYAADG
QDLFVRLAAA EFGERRTIRG KIIGLIIGIS LMLVLSFIIY CFWKKKQKRA RATAAPIGYR
DRIQELIITN GVVMSSGRRL LGEEEDLELP LTEFETVVMA TENFSDSNIL GRGGFGIVYK
GRLLDG
