GCAL1_ARATH
ID GCAL1_ARATH Reviewed; 252 AA.
AC Q9FMV1; Q8LBM1; Q93XY3;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Gamma carbonic anhydrase-like 1, mitochondrial;
DE Short=AtCAL1;
DE Short=GAMMA CAL1;
DE Flags: Precursor;
GN Name=GAMMACAL1; OrderedLocusNames=At5g63510; ORFNames=MLE2.14;
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 {ECO:0000312|EMBL:BAB08816.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [2] {ECO:0000305}
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] {ECO:0000305}
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] {ECO:0000305}
RP PROTEIN SEQUENCE OF 174-186, AND SUBCELLULAR LOCATION.
RC TISSUE=Leaf, and Stem;
RX PubMed=11743114; DOI=10.1104/pp.010474;
RA Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.;
RT "Proteomic approach to identify novel mitochondrial proteins in
RT Arabidopsis.";
RL Plant Physiol. 127:1694-1710(2001).
RN [6]
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).
RN [7]
RP INTERACTION WITH GAMMACA2, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15821992; DOI=10.1007/s11103-004-6324-z;
RA Perales M., Parisi G., Fornasari M.S., Colaneri A., Villarreal F.,
RA Gonzalez-Schain N., Echave J., Gomez-Casati D., Braun H.-P., Araya A.,
RA Zabaleta E.;
RT "Gamma carbonic anhydrase like complex interact with plant mitochondrial
RT complex I.";
RL Plant Mol. Biol. 56:947-957(2004).
CC -!- FUNCTION: Involved in complex I assembly in mitochondria and
CC respiration.
CC -!- SUBUNIT: Component of the mitochondrial oxidoreductase respiratory
CC chain complex I; element of the extra matrix-exposed domain, which is
CC attached to the membrane arm of this complex. Interacts with GAMMACA2.
CC {ECO:0000269|PubMed:15821992}.
CC -!- INTERACTION:
CC Q9FMV1; Q9C6B3: GAMMACA2; NbExp=2; IntAct=EBI-532008, EBI-531995;
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:11743114, ECO:0000269|PubMed:14671022,
CC ECO:0000269|PubMed:15821992}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11743114, ECO:0000269|PubMed:14671022,
CC ECO:0000269|PubMed:15821992}; Matrix side {ECO:0000269|PubMed:11743114,
CC ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:15821992}.
CC Note=Probably integral to the membrane. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FMV1-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the gamma-class carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; AB007649; BAB08816.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97760.1; -; Genomic_DNA.
DR EMBL; AY054587; AAK96778.1; -; mRNA.
DR EMBL; AY064687; AAL47391.1; -; mRNA.
DR EMBL; AY087124; AAM64682.1; -; mRNA.
DR RefSeq; NP_201156.1; NM_125746.4. [Q9FMV1-1]
DR PDB; 7A23; EM; 3.70 A; o=1-252.
DR PDB; 7A24; EM; 3.80 A; o=1-252.
DR PDBsum; 7A23; -.
DR PDBsum; 7A24; -.
DR AlphaFoldDB; Q9FMV1; -.
DR SMR; Q9FMV1; -.
DR BioGRID; 21712; 34.
DR IntAct; Q9FMV1; 2.
DR STRING; 3702.AT5G63510.2; -.
DR iPTMnet; Q9FMV1; -.
DR PRIDE; Q9FMV1; -.
DR ProteomicsDB; 221887; -. [Q9FMV1-1]
DR EnsemblPlants; AT5G63510.1; AT5G63510.1; AT5G63510. [Q9FMV1-1]
DR GeneID; 836470; -.
DR Gramene; AT5G63510.1; AT5G63510.1; AT5G63510. [Q9FMV1-1]
DR KEGG; ath:AT5G63510; -.
DR Araport; AT5G63510; -.
DR HOGENOM; CLU_064827_0_1_1; -.
DR InParanoid; Q9FMV1; -.
DR PhylomeDB; Q9FMV1; -.
DR BioCyc; ARA:AT5G63510-MON; -.
DR BioCyc; MetaCyc:AT5G63510-MON; -.
DR BRENDA; 4.2.1.1; 399.
DR PRO; PR:Q9FMV1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMV1; baseline and differential.
DR Genevisible; Q9FMV1; AT.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR SUPFAM; SSF51161; SSF51161; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing; Membrane;
KW Metal-binding; Mitochondrion; Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..252
FT /note="Gamma carbonic anhydrase-like 1, mitochondrial"
FT /id="PRO_0000220588"
FT BINDING 99..101
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 114..115
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="R -> L (in Ref. 4; AAM64682)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="E -> G (in Ref. 3; AAK96778/AAL47391)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="V -> L (in Ref. 4; AAM64682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 252 AA; 27570 MW; B718E71B22ACC4A7 CRC64;
MATSIARLSR RGVTSNLIRR CFAAEAALAR KTELPKPQFT VSPSTDRVKW DYRGQRQIIP
LGQWLPKVAV DAYVAPNVVL AGQVTVWDGS SVWNGAVLRG DLNKITVGFC SNVQERCVVH
AAWSSPTGLP AATIIDRYVT VGAYSLLRSC TIEPECIIGQ HSILMEGSLV ETRSILEAGS
VVPPGRRIPS GELWGGNPAR FIRTLTNEET LEIPKLAVAI NHLSGDYFSE FLPYSTVYLE
VEKFKKSLGI AV
