PHB5_ARATH
ID PHB5_ARATH Reviewed; 249 AA.
AC Q9LY99;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Prohibitin-5, mitochondrial;
DE Short=Atphb5;
GN Name=PHB5; OrderedLocusNames=At5g14300; ORFNames=F18O22.90;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
CC -!- FUNCTION: Prohibitin probably acts as a holdase/unfoldase for the
CC stabilization of newly synthesized mitochondrial proteins.
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of a prohibitin multimeric complex in mitochondrial
CC membranes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14671022}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:14671022}.
CC -!- SIMILARITY: Belongs to the prohibitin family. {ECO:0000305}.
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DR EMBL; AL163817; CAB87769.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92014.1; -; Genomic_DNA.
DR PIR; T48603; T48603.
DR RefSeq; NP_196934.1; NM_121434.1.
DR AlphaFoldDB; Q9LY99; -.
DR SMR; Q9LY99; -.
DR BioGRID; 16557; 28.
DR STRING; 3702.AT5G14300.1; -.
DR PaxDb; Q9LY99; -.
DR PRIDE; Q9LY99; -.
DR EnsemblPlants; AT5G14300.1; AT5G14300.1; AT5G14300.
DR GeneID; 831280; -.
DR Gramene; AT5G14300.1; AT5G14300.1; AT5G14300.
DR KEGG; ath:AT5G14300; -.
DR Araport; AT5G14300; -.
DR TAIR; locus:2145718; AT5G14300.
DR eggNOG; KOG3083; Eukaryota.
DR HOGENOM; CLU_047969_0_0_1; -.
DR InParanoid; Q9LY99; -.
DR OMA; THRKIPW; -.
DR OrthoDB; 1089994at2759; -.
DR PhylomeDB; Q9LY99; -.
DR PRO; PR:Q9LY99; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LY99; differential.
DR Genevisible; Q9LY99; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR CDD; cd03401; SPFH_prohibitin; 1.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR000163; Prohibitin.
DR PANTHER; PTHR23222; PTHR23222; 2.
DR Pfam; PF01145; Band_7; 2.
DR PRINTS; PR00679; PROHIBITIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..249
FT /note="Prohibitin-5, mitochondrial"
FT /id="PRO_0000420600"
FT TOPO_DOM 1..8
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..249
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
SQ SEQUENCE 249 AA; 27392 MW; FAFCC3412047D5E4 CRC64;
MPWSKFTKVA LGLGAAIAAV RSTMFTVDGG QRAVMFHRFE GILEEPVGEG THRKIPWVQK
PYIFDIRTKP YKINTDSGTK DLQMVNLTLR VMFRPDVVKA VVAQFNADEL LTERPQVSAL
IRETLIKRAK EFNIVLDDVS ITGLSYGKEF SLAVERKQVA QQEAERSKFV VAKADQERRA
AVIRAEGESE AARVISKATA GAGMGLIKLR RVEAAREVAI TLSNSPNVVY LPSGGNMLFA
MNGPSKVVA
