SODC3_DICDI
ID SODC3_DICDI Reviewed; 407 AA.
AC Q54RQ1; Q52KB2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Extracellular superoxide dismutase [Cu-Zn] 3;
DE Short=EC-SOD 3;
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=sodC; ORFNames=DDB_G0282993;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP IDENTIFICATION.
RX PubMed=12913271; DOI=10.1248/bpb.26.1174;
RA Tsuji A., Akaza Y., Nakamura S., Kodaira K., Yasukawa H.;
RT "Multinucleation of the sodC-deficient Dictyostelium discoideum.";
RL Biol. Pharm. Bull. 26:1174-1177(2003).
CC -!- FUNCTION: Protect the extracellular space from toxic effect of reactive
CC oxygen intermediates by converting superoxyde radicals into hydrogen
CC peroxyde and oxygen. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:18421; EC=1.15.1.1;
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000049; EAL65940.1; -; Genomic_DNA.
DR EMBL; BR000218; FAA00020.1; -; mRNA.
DR RefSeq; XP_639300.1; XM_634208.1.
DR AlphaFoldDB; Q54RQ1; -.
DR SMR; Q54RQ1; -.
DR STRING; 44689.DDB0232186; -.
DR PaxDb; Q54RQ1; -.
DR EnsemblProtists; EAL65940; EAL65940; DDB_G0282993.
DR GeneID; 8623871; -.
DR KEGG; ddi:DDB_G0282993; -.
DR dictyBase; DDB_G0282993; sodC.
DR eggNOG; KOG0441; Eukaryota.
DR HOGENOM; CLU_676923_0_0_1; -.
DR InParanoid; Q54RQ1; -.
DR OMA; RGMAVHN; -.
DR Reactome; R-DDI-3299685; Detoxification of Reactive Oxygen Species.
DR PRO; PR:Q54RQ1; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0071476; P:cellular hypotonic response; IMP:dictyBase.
DR GO; GO:0009267; P:cellular response to starvation; IEP:dictyBase.
DR GO; GO:0033298; P:contractile vacuole organization; IDA:dictyBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:dictyBase.
DR GO; GO:0032880; P:regulation of protein localization; IMP:dictyBase.
DR GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IEP:dictyBase.
DR Gene3D; 2.60.40.200; -; 2.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR InterPro; IPR018152; SOD_Cu/Zn_BS.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR InterPro; IPR031078; SodC2/C3-like.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR PANTHER; PTHR10003:SF73; PTHR10003:SF73; 1.
DR Pfam; PF00080; Sod_Cu; 2.
DR SUPFAM; SSF49329; SSF49329; 2.
DR PROSITE; PS00087; SOD_CU_ZN_1; 1.
PE 2: Evidence at transcript level;
KW Antioxidant; Cell membrane; Copper; Glutathionylation; Glycoprotein;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..407
FT /note="Extracellular superoxide dismutase [Cu-Zn] 3"
FT /id="PRO_0000327853"
FT TOPO_DOM 20..386
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 245
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 68
FT /note="A -> V (in Ref. 1; FAA00020)"
FT /evidence="ECO:0000305"
FT CONFLICT 352..353
FT /note="LP -> HT (in Ref. 1; FAA00020)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 43572 MW; F969421CE55F4F17 CRC64;
MRLLSVLVFL ISVISIAKAD YQYAFCKFNE LSIGGVEGIA HLLSTDGTTL NITFDFTTSY
AQNTQFAAQI LTYGYNPSSM TNLGSVFDPT NVKTAGCPSG TPRAGDIGNI QANGGNVEAQ
TISLNIPNIK DDANSIIGRS IAIYGGSYDC SDPSKSVIGD MISFCTIGVG NIDYSSFDKS
KLTGVNTASS YSNLENAIGL AVVYNTTITK GDYIEGRVLF KALNSSFIQV SAKVSGLSYQ
AHGFHVHQFG DVSSDNGTSI GGHFLKTGQE HSLPPSGTRH YGDFGNFCAF SQDMMDTGYY
YYETDHVTAA LVIGRGMAVH NFTDKGNSDV GGSRCGQGVI ALIQDADYSL NLPMDWKWDV
ICANGSYYGD MSTSMNSESY NDNEPGSSST VIPFFALIIF SIIFALL
