PAM68_ARATH
ID PAM68_ARATH Reviewed; 214 AA.
AC O49668;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Protein PAM68, chloroplastic;
DE AltName: Full=PHOTOSYNTHESIS AFFECTED MUTANT 68;
DE Flags: Precursor;
GN Name=PAM68; OrderedLocusNames=At4g19100; ORFNames=T18B16.70;
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 [MRNA].
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH PSBA; PSBB;
RP PSBC; PSBD; PSBH; PSBI; HCF136; LPA1; LPA2 AND ALB3, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20923938; DOI=10.1105/tpc.110.077453;
RA Armbruster U., Zuhlke J., Rengstl B., Kreller R., Makarenko E., Ruhle T.,
RA Schunemann D., Jahns P., Weisshaar B., Nickelsen J., Leister D.;
RT "The Arabidopsis thylakoid protein PAM68 is required for efficient D1
RT biogenesis and photosystem II assembly.";
RL Plant Cell 22:3439-3460(2010).
CC -!- FUNCTION: Involved in early steps in photosystem II (PSII) biogenesis
CC and in maturation and stability of newly synthesized psbA protein.
CC {ECO:0000269|PubMed:20923938}.
CC -!- SUBUNIT: Interacts with the PSII subunits psbA, psbB, psbC, psbD, psbH
CC and psbI, but not with psbE, psbF or psbO. Interacts with the PSII
CC assembly factors HCF136, LPA1, LPA2 and ALB3.
CC {ECO:0000269|PubMed:20923938}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:20923938}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20923938}.
CC -!- DISRUPTION PHENOTYPE: Strongly reduced growth. Pale-green cotyledons
CC and leaves. {ECO:0000269|PubMed:20923938}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT029521; ABL66777.1; -; mRNA.
DR EMBL; AL021687; CAA16699.1; -; Genomic_DNA.
DR EMBL; AL161550; CAB78912.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84140.1; -; Genomic_DNA.
DR PIR; T04431; T04431.
DR RefSeq; NP_974571.1; NM_202842.3.
DR AlphaFoldDB; O49668; -.
DR STRING; 3702.AT4G19100.1; -.
DR iPTMnet; O49668; -.
DR PaxDb; O49668; -.
DR PRIDE; O49668; -.
DR ProteomicsDB; 248634; -.
DR EnsemblPlants; AT4G19100.1; AT4G19100.1; AT4G19100.
DR GeneID; 2745715; -.
DR Gramene; AT4G19100.1; AT4G19100.1; AT4G19100.
DR KEGG; ath:AT4G19100; -.
DR Araport; AT4G19100; -.
DR TAIR; locus:1006589876; AT4G19100.
DR eggNOG; ENOG502RXKE; Eukaryota.
DR HOGENOM; CLU_099250_0_0_1; -.
DR InParanoid; O49668; -.
DR OrthoDB; 1629732at2759; -.
DR PhylomeDB; O49668; -.
DR BioCyc; MetaCyc:MON-16601; -.
DR PRO; PR:O49668; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49668; baseline and differential.
DR Genevisible; O49668; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR GO; GO:0010207; P:photosystem II assembly; IMP:TAIR.
DR InterPro; IPR021855; PAM68-like.
DR PANTHER; PTHR34575; PTHR34575; 1.
DR Pfam; PF11947; DUF3464; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Membrane; Photosynthesis; Photosystem II; Plastid;
KW Reference proteome; Thylakoid; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..35
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 36..214
FT /note="Protein PAM68, chloroplastic"
FT /id="PRO_0000403964"
FT TOPO_DOM 36..124
FT /note="Stromal"
FT /evidence="ECO:0000269|PubMed:20923938"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..152
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000269|PubMed:20923938"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..214
FT /note="Stromal"
FT /evidence="ECO:0000269|PubMed:20923938"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..108
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 214 AA; 24212 MW; 7E92404A98CE1F8C CRC64;
MASVPCSFKL SAHRRSSSKL DGNNKQCSSL VERLRDKTKS QVPKSITCIN RLEISRIAPL
HATMNSPKGF GPPPKKTKKS KKPKPGNQSD EDDDDEDEDD DDEEDERERG VIPEIVTNRM
ISRMGFTVGL PLFIGLLFFP FFYYLKVGLK VDVPTWVPFI VSFVFFGTAL AGVSYGIVSS
SWDPLREGSL LGWNEAKKNW PVFWQSFWNS SDKR
