GCAL2_ARATH
ID GCAL2_ARATH Reviewed; 256 AA.
AC Q9SMN1;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Gamma carbonic anhydrase-like 2, mitochondrial;
DE Short=AtCAL2;
DE Short=GAMMA CAL2;
DE Flags: Precursor;
GN Name=GAMMACAL2; OrderedLocusNames=At3g48680; ORFNames=T8P19.190;
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:AAK25924.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 PROTEIN SEQUENCE OF 31-36; 192-204 AND 208-219, 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 [5]
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 [6]
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).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16407270; DOI=10.1074/jbc.m511542200;
RA Sunderhaus S., Dudkina N.V., Jaensch L., Klodmann J., Heinemeyer J.,
RA Perales M., Zabaleta E., Boekema E.J., Braun H.-P.;
RT "Carbonic anhydrase subunits form a matrix-exposed domain attached to the
RT membrane arm of mitochondrial complex I in plants.";
RL J. Biol. Chem. 281:6482-6488(2006).
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 Q9SMN1; Q9C6B3: GAMMACA2; NbExp=3; IntAct=EBI-532001, EBI-531995;
CC Q9SMN1; Q9LRH6: GATA25; NbExp=3; IntAct=EBI-532001, EBI-2460434;
CC Q9SMN1; Q8GXW1: RGL2; NbExp=3; IntAct=EBI-532001, EBI-963665;
CC Q9SMN1; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-532001, EBI-4426557;
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 -!- SIMILARITY: Belongs to the gamma-class carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; AL133315; CAB62357.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78445.1; -; Genomic_DNA.
DR EMBL; AF360214; AAK25924.1; -; mRNA.
DR EMBL; AY051017; AAK93694.1; -; mRNA.
DR PIR; T46212; T46212.
DR RefSeq; NP_190437.1; NM_114727.4.
DR PDB; 7AQQ; EM; 3.06 A; x=1-256.
DR PDB; 7AR7; EM; 3.72 A; x=41-254.
DR PDB; 7AR8; EM; 3.53 A; x=1-256.
DR PDB; 7ARB; EM; 3.41 A; x=1-256.
DR PDBsum; 7AQQ; -.
DR PDBsum; 7AR7; -.
DR PDBsum; 7AR8; -.
DR PDBsum; 7ARB; -.
DR AlphaFoldDB; Q9SMN1; -.
DR SMR; Q9SMN1; -.
DR BioGRID; 9347; 39.
DR IntAct; Q9SMN1; 6.
DR STRING; 3702.AT3G48680.1; -.
DR iPTMnet; Q9SMN1; -.
DR PaxDb; Q9SMN1; -.
DR PRIDE; Q9SMN1; -.
DR ProteomicsDB; 221888; -.
DR EnsemblPlants; AT3G48680.1; AT3G48680.1; AT3G48680.
DR GeneID; 824029; -.
DR Gramene; AT3G48680.1; AT3G48680.1; AT3G48680.
DR KEGG; ath:AT3G48680; -.
DR Araport; AT3G48680; -.
DR TAIR; locus:2114445; AT3G48680.
DR eggNOG; ENOG502QQV5; Eukaryota.
DR HOGENOM; CLU_064827_0_1_1; -.
DR InParanoid; Q9SMN1; -.
DR OMA; ERCVIME; -.
DR OrthoDB; 1270774at2759; -.
DR PhylomeDB; Q9SMN1; -.
DR BioCyc; ARA:AT3G48680-MON; -.
DR BioCyc; MetaCyc:AT3G48680-MON; -.
DR BRENDA; 4.2.1.1; 399.
DR PRO; PR:Q9SMN1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SMN1; baseline and differential.
DR Genevisible; Q9SMN1; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:TAIR.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0045271; C:respiratory chain complex I; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009853; P:photorespiration; TAS:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IGI:TAIR.
DR GO; GO:0009651; P:response to salt stress; IGI:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IGI:TAIR.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR SUPFAM; SSF51161; SSF51161; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Membrane; Metal-binding;
KW Mitochondrion; Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..256
FT /note="Gamma carbonic anhydrase-like 2, mitochondrial"
FT /id="PRO_0000220589"
FT BINDING 103..105
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 118..119
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 101..111
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:7AQQ"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 211..232
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 241..251
FT /evidence="ECO:0007829|PDB:7AQQ"
SQ SEQUENCE 256 AA; 27956 MW; 3AFB1905F4EEA2D1 CRC64;
MATSLARISK RSITSAVSSN LIRRYFAAEA VAVATTETPK PKSQVTPSPD RVKWDYRGQR
QIIPLGQWLP KVAVDAYVAP NVVLAGQVTV WDGSSVWNGA VLRGDLNKIT VGFCSNVQER
CVVHAAWSSP TGLPAQTLID RYVTVGAYSL LRSCTIEPEC IIGQHSILME GSLVETRSIL
EAGSVLPPGR RIPSGELWGG NPARFIRTLT NEETLEIPKL AVAINHLSGD YFSEFLPYST
IYLEVEKFKK SLGIAI
