CCMH_ARATH
ID CCMH_ARATH Reviewed; 159 AA.
AC Q9XI46;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cytochrome c-type biogenesis CcmH-like mitochondrial protein {ECO:0000305};
DE Short=AtCCMH {ECO:0000303|PubMed:16236729};
GN Name=CCMH {ECO:0000303|PubMed:16236729};
GN OrderedLocusNames=At1g15220 {ECO:0000312|Araport:AT1G15220};
GN ORFNames=F9L1.17 {ECO:0000312|EMBL:AAD39651.1};
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, INTERACTION WITH CYTC-1, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=16236729; DOI=10.1073/pnas.0503473102;
RA Meyer E.H., Giege P., Gelhaye E., Rayapuram N., Ahuja U., Thony-Meyer L.,
RA Grienenberger J.M., Bonnard G.;
RT "AtCCMH, an essential component of the c-type cytochrome maturation pathway
RT in Arabidopsis mitochondria, interacts with apocytochrome c.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16113-16118(2005).
RN [6]
RP FUNCTION, AND INTERACTION WITH CCMFN1 AND CCMFN2.
RX PubMed=18644794; DOI=10.1074/jbc.m802621200;
RA Rayapuram N., Hagenmuller J., Grienenberger J.M., Bonnard G., Giege P.;
RT "The three mitochondrial encoded CcmF proteins form a complex that
RT interacts with CCMH and c-type apocytochromes in Arabidopsis.";
RL J. Biol. Chem. 283:25200-25208(2008).
CC -!- FUNCTION: Plays a central role in mitochondrial cytochrome c
CC maturation. Probable component of a heme lyase complex involved in the
CC reduction of apocytochrome c (PubMed:16236729). Forms a complex with
CC CCMF proteins (CCMFC, CCMFN1 and CCMFN2) that performs the assembly of
CC heme with c-type apocytochromes in mitochondria (PubMed:18644794).
CC {ECO:0000269|PubMed:16236729, ECO:0000269|PubMed:18644794}.
CC -!- SUBUNIT: Interacts (via N-terminus) with CYTC-1 (PubMed:16236729).
CC Interacts with CCMFN1 and CCMFN2 (PubMed:18644794).
CC {ECO:0000269|PubMed:16236729, ECO:0000269|PubMed:18644794}.
CC -!- INTERACTION:
CC Q9XI46; Q33884: CCMFN2; NbExp=3; IntAct=EBI-763363, EBI-763400;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:16236729}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous. Arrest of
CC embryo development at the torpedo stage. {ECO:0000269|PubMed:16236729}.
CC -!- SIMILARITY: Belongs to the CcmH/CycL/Ccl2/NrfF family. {ECO:0000305}.
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DR EMBL; AC007591; AAD39651.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29289.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29290.1; -; Genomic_DNA.
DR EMBL; AY050392; AAK91409.1; -; mRNA.
DR EMBL; AY097355; AAM19871.1; -; mRNA.
DR EMBL; AY085498; AAM62723.1; -; mRNA.
DR PIR; D86286; D86286.
DR RefSeq; NP_563966.1; NM_101390.2.
DR RefSeq; NP_973834.1; NM_202105.2.
DR AlphaFoldDB; Q9XI46; -.
DR SMR; Q9XI46; -.
DR IntAct; Q9XI46; 4.
DR STRING; 3702.AT1G15220.2; -.
DR PaxDb; Q9XI46; -.
DR PRIDE; Q9XI46; -.
DR ProteomicsDB; 223918; -.
DR EnsemblPlants; AT1G15220.1; AT1G15220.1; AT1G15220.
DR EnsemblPlants; AT1G15220.2; AT1G15220.2; AT1G15220.
DR GeneID; 838089; -.
DR Gramene; AT1G15220.1; AT1G15220.1; AT1G15220.
DR Gramene; AT1G15220.2; AT1G15220.2; AT1G15220.
DR KEGG; ath:AT1G15220; -.
DR Araport; AT1G15220; -.
DR TAIR; locus:2037718; AT1G15220.
DR eggNOG; ENOG502RXFW; Eukaryota.
DR HOGENOM; CLU_107187_1_0_1; -.
DR InParanoid; Q9XI46; -.
DR OMA; WAYNRHR; -.
DR OrthoDB; 1334229at2759; -.
DR PhylomeDB; Q9XI46; -.
DR PRO; PR:Q9XI46; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XI46; baseline and differential.
DR Genevisible; Q9XI46; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0032991; C:protein-containing complex; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:TAIR.
DR GO; GO:0017004; P:cytochrome complex assembly; TAS:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR Gene3D; 1.10.8.640; -; 1.
DR InterPro; IPR005616; CcmH/CycL/Ccl2/NrfF.
DR InterPro; IPR038297; CcmH/CycL/NrfF/Ccl2_sf.
DR Pfam; PF03918; CcmH; 1.
PE 1: Evidence at protein level;
KW Cytochrome c-type biogenesis; Heme; Iron; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..159
FT /note="Cytochrome c-type biogenesis CcmH-like mitochondrial
FT protein"
FT /id="PRO_0000432846"
FT TOPO_DOM 1..82
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:16236729"
FT TRANSMEM 83..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..159
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:16236729"
FT BINDING 27
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:16236729"
FT BINDING 30
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:16236729"
SQ SEQUENCE 159 AA; 17885 MW; 51637FB6AFD683F7 CRC64;
MEKTDEERKK AQMLDARARN ISHNVRCTEC GSQSIEDSQA DIAILLRQLI RNEIGAGKTD
KEIYSKLEDE FGETVLYAPK FDLQTAALWL TPVIIAGGTA AGIVYQKHRL RKNVDIMALN
LIRGVPLTPK ERVTILDVLI PPSPPPQGVV SRLRRWLNR
