CHM1B_ARATH
ID CHM1B_ARATH Reviewed; 203 AA.
AC Q9SSM4; Q8LFG3;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=ESCRT-related protein CHMP1B {ECO:0000305};
DE AltName: Full=Protein CHARGED MULTIVESICULAR BODY PROTEIN 1B {ECO:0000303|PubMed:19304934};
DE AltName: Full=Protein CHROMATIN MODIFYING PROTEIN 1B {ECO:0000303|PubMed:19304934};
DE AltName: Full=Vacuolar protein-sorting-associated protein 46.2 {ECO:0000312|EMBL:AEE35406.1};
GN Name=CHMP1B {ECO:0000303|PubMed:19304934};
GN Synonyms=VPS46.2 {ECO:0000312|EMBL:AEE35406.1};
GN OrderedLocusNames=At1g73030 {ECO:0000312|Araport:AT1G73030};
GN ORFNames=F3N23.23 {ECO:0000312|EMBL:AAD55650.1};
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19304934; DOI=10.1105/tpc.108.064865;
RA Spitzer C., Reyes F.C., Buono R., Sliwinski M.K., Haas T.J., Otegui M.S.;
RT "The ESCRT-related CHMP1A and B proteins mediate multivesicular body
RT sorting of auxin carriers in Arabidopsis and are required for plant
RT development.";
RL Plant Cell 21:749-766(2009).
RN [6]
RP INTERACTION WITH CHMP1A AND LIP5.
RC STRAIN=cv. Columbia;
RX PubMed=20663085; DOI=10.1111/j.1365-313x.2010.04310.x;
RA Shahriari M., Keshavaiah C., Scheuring D., Sabovljevic A., Pimpl P.,
RA Haeusler R.E., Huelskamp M., Schellmann S.;
RT "The AAA-type ATPase AtSKD1 contributes to vacuolar maintenance of
RT Arabidopsis thaliana.";
RL Plant J. 64:71-85(2010).
RN [7]
RP INTERACTION WITH VPS2.2.
RX PubMed=22010978; DOI=10.1021/pr200845n;
RA Ibl V., Csaszar E., Schlager N., Neubert S., Spitzer C., Hauser M.T.;
RT "Interactome of the plant-specific ESCRT-III component AtVPS2.2 in
RT Arabidopsis thaliana.";
RL J. Proteome Res. 11:397-411(2012).
RN [8]
RP FUNCTION.
RX PubMed=25649438; DOI=10.1105/tpc.114.135939;
RA Spitzer C., Li F., Buono R., Roschzttardtz H., Chung T., Zhang M.,
RA Osteryoung K.W., Vierstra R.D., Otegui M.S.;
RT "The endosomal protein CHARGED MULTIVESICULAR BODY PROTEIN1 regulates the
RT autophagic turnover of plastids in Arabidopsis.";
RL Plant Cell 27:391-402(2015).
CC -!- FUNCTION: Involved in ESCRT-dependent multivesicular body (MVB)
CC formation and sorting of endosomal cargo proteins into MVBs. Mediates
CC the MVB sorting of the auxin carriers PIN1, PIN2 and AUX1. Required for
CC embryonic axis establishment and seedling growth (PubMed:19304934).
CC Required for autophagic degradation of plastid proteins. Promotes the
CC efficient sequestration of cargo from plastids into autophagosomes.
CC Mediates the efficient delivery of autophagic plastid bodies to the
CC vacuole, but not into the cytoplasm (PubMed:25649438).
CC {ECO:0000269|PubMed:19304934, ECO:0000269|PubMed:25649438}.
CC -!- SUBUNIT: Interacts with CHMP1A and LIP5 (PubMed:20663085). Interacts
CC with VPS2.2 (PubMed:22010978). {ECO:0000269|PubMed:20663085,
CC ECO:0000269|PubMed:22010978}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HD42}.
CC Endosome membrane {ECO:0000250|UniProtKB:Q9HD42}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q9HD42}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but double mutants chmp1a and chmp1b show embryo
CC development defect. {ECO:0000269|PubMed:19304934}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; AC008017; AAD55650.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35406.1; -; Genomic_DNA.
DR EMBL; AY059851; AAL24333.1; -; mRNA.
DR EMBL; AY081673; AAM10235.1; -; mRNA.
DR EMBL; AY084868; AAM61431.1; -; mRNA.
DR PIR; G96755; G96755.
DR RefSeq; NP_565053.1; NM_105961.3.
DR AlphaFoldDB; Q9SSM4; -.
DR SMR; Q9SSM4; -.
DR IntAct; Q9SSM4; 3.
DR STRING; 3702.AT1G73030.1; -.
DR TCDB; 3.A.31.1.2; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR PaxDb; Q9SSM4; -.
DR PRIDE; Q9SSM4; -.
DR ProteomicsDB; 241028; -.
DR EnsemblPlants; AT1G73030.1; AT1G73030.1; AT1G73030.
DR GeneID; 843634; -.
DR Gramene; AT1G73030.1; AT1G73030.1; AT1G73030.
DR KEGG; ath:AT1G73030; -.
DR Araport; AT1G73030; -.
DR TAIR; locus:2032607; AT1G73030.
DR eggNOG; KOG3232; Eukaryota.
DR HOGENOM; CLU_080826_0_1_1; -.
DR InParanoid; Q9SSM4; -.
DR OMA; VMDRFET; -.
DR OrthoDB; 1441797at2759; -.
DR PhylomeDB; Q9SSM4; -.
DR PRO; PR:Q9SSM4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SSM4; baseline and differential.
DR Genevisible; Q9SSM4; AT.
DR GO; GO:0000815; C:ESCRT III complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IGI:TAIR.
DR GO; GO:0000578; P:embryonic axis specification; IGI:TAIR.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IGI:TAIR.
DR GO; GO:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0090351; P:seedling development; IGI:TAIR.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR10476; PTHR10476; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Endosome; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..203
FT /note="ESCRT-related protein CHMP1B"
FT /id="PRO_0000433027"
FT REGION 172..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 13..51
FT /evidence="ECO:0000255"
FT COILED 109..140
FT /evidence="ECO:0000255"
FT COMPBIAS 181..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 63
FT /note="S -> R (in Ref. 4; AAM61431)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 203 AA; 22691 MW; 7E56E8D937B38CD2 CRC64;
MGNTDKLMNQ IFDLKFTSKS LQRQSRKCEK EEKAEKLKVK KAIEKGNMDG ARIYAENAIR
KRSEQMNYLR LASRLDAVVA RLDTQAKMTT ITKSMTNIVK SLESSLATGN LQKMSETMDS
FEKQFVNMEV QAEFMENAMA GSTSLSTPEG EVNSLMQQVA DDYGLEVSVG LPQPAGHAIP
TKTEEKVDED DLSRRLAELK ARG
