LOCUS NP_001075295 154 aa linear MAM 23-OCT-2017
DEFINITION superoxide dismutase [Cu-Zn] [Equus caballus].
ACCESSION NP_001075295
VERSION NP_001075295.1
DBSOURCE REFSEQ: accession NM_001081826.3
KEYWORDS RefSeq.
SOURCE Equus caballus (horse)
ORGANISM Equus caballus
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
REFERENCE 1 (residues 1 to 154)
AUTHORS Hestand MS, Kalbfleisch TS, Coleman SJ, Zeng Z, Liu J, Orlando L
and MacLeod JN.
TITLE Annotation of the Protein Coding Regions of the Equine Genome
JOURNAL PLoS ONE 10 (6), E0124375 (2015)
PUBMED 26107351
REMARK Publication Status: Online-Only
REFERENCE 2 (residues 1 to 154)
AUTHORS Ishida N, Katayama Y, Sato F, Hasegawa T and Mukoyama H.
TITLE The cDNA sequences of equine antioxidative enzyme genes Cu/Zn-SOD
and Mn-SOD, and these expressions in equine tissues
JOURNAL J. Vet. Med. Sci. 61 (3), 291-294 (1999)
PUBMED 10331206
REFERENCE 3 (residues 1 to 154)
AUTHORS de la Rua-Domenech R, Wiedmann M, Mohammed HO, Cummings JF, Divers
TJ and Batt CA.
TITLE Equine motor neuron disease is not linked to Cu/Zn superoxide
dismutase mutations: sequence analysis of the equine Cu/Zn
superoxide dismutase cDNA
JOURNAL Gene 178 (1-2), 83-88 (1996)
PUBMED 8921896
REFERENCE 4 (residues 1 to 154)
AUTHORS Lerch,K. and Ammer,D.
TITLE Amino acid sequence of copper-zinc superoxide dismutase from horse
liver
JOURNAL J. Biol. Chem. 256 (22), 11545-11551 (1981)
PUBMED 7298616
COMMENT VALIDATED REFSEQ: This record has undergone validation or
preliminary review. The reference sequence was derived from
AAWR02022876.1 and GU808339.1.
Sequence Note: This RefSeq record was created from transcript and
genomic sequence data to make the sequence consistent with the
reference genome assembly. The genomic coordinates used for the
transcript record were based on transcript alignments.
##Evidence-Data-START##
Transcript exon combination :: GU808339.1, AB001692.1 [ECO:0000332]
RNAseq introns :: single sample supports all introns
SAMEA2008637, SAMEA2452530
[ECO:0000348]
##Evidence-Data-END##
FEATURES Location/Qualifiers
source 1..154
/organism="Equus caballus"
/db_xref="taxon:9796"
/chromosome="26"
/map="26"
Protein 1..154
/product="superoxide dismutase [Cu-Zn]"
/EC_number="1.15.1.1"
/note="Cu/Zn superoxide dismutase; superoxide dismutase 1,
soluble"
/calculated_mol_wt=15940
Site 2
/site_type="acetylation"
/experiment="experimental evidence, no additional details
recorded"
/note="N-acetylalanine. {ECO:0000269|PubMed:7298616};
propagated from UniProtKB/Swiss-Prot (P00443.2)"
Region 4..147
/region_name="Cu-Zn_Superoxide_Dismutase"
/note="Copper/zinc superoxide dismutase (SOD). superoxide
dismutases catalyse the conversion of superoxide radicals
to molecular oxygen. Three evolutionarily distinct
families of SODs are known, of which the
copper/zinc-binding family is one. Defects in the...;
cd00305"
/db_xref="CDD:238186"
Site 4
/site_type="modified"
/experiment="experimental evidence, no additional details
recorded"
/note="N6-succinyllysine. {ECO:0000250|UniProtKB:P08228};
propagated from UniProtKB/Swiss-Prot (P00443.2)"
Site order(6,8,18,20,51..53,114..115)
/site_type="other"
/note="E-class dimer interface [polypeptide binding]"
/db_xref="CDD:238186"
Site 10
/site_type="modified"
/experiment="experimental evidence, no additional details
recorded"
/note="N6-succinyllysine. {ECO:0000250|UniProtKB:P08228};
propagated from UniProtKB/Swiss-Prot (P00443.2)"
Site order(31,89)
/site_type="other"
/note="P-class dimer interface [polypeptide binding]"
/db_xref="CDD:238186"
Site order(47,49,64,81,84,121)
/site_type="active"
/db_xref="CDD:238186"
Site order(47,49,64,121)
/site_type="other"
/note="Cu2+ binding site [ion binding]"
/db_xref="CDD:238186"
Site order(64,72,81,84)
/site_type="other"
/note="Zn2+ binding site [ion binding]"
/db_xref="CDD:238186"
Site 103
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/note="Phosphoserine. {ECO:0000250|UniProtKB:P00441};
propagated from UniProtKB/Swiss-Prot (P00443.2)"
Site 106
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/note="Phosphoserine. {ECO:0000250|UniProtKB:P07632};
propagated from UniProtKB/Swiss-Prot (P00443.2)"
Site 108
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/note="Phosphoserine. {ECO:0000250|UniProtKB:P08228};
propagated from UniProtKB/Swiss-Prot (P00443.2)"
Site 123
/site_type="acetylation"
/experiment="experimental evidence, no additional details
recorded"
/note="N6-acetyllysine, alternate.
{ECO:0000250|UniProtKB:P00441}; propagated from
UniProtKB/Swiss-Prot (P00443.2)"
Site 123
/site_type="modified"
/experiment="experimental evidence, no additional details
recorded"
/note="N6-succinyllysine, alternate.
{ECO:0000250|UniProtKB:P00441}; propagated from
UniProtKB/Swiss-Prot (P00443.2)"
Site 137
/site_type="acetylation"
/experiment="experimental evidence, no additional details
recorded"
/note="N6-acetyllysine, alternate.
{ECO:0000250|UniProtKB:P08228}; propagated from
UniProtKB/Swiss-Prot (P00443.2)"
Site 137
/site_type="modified"
/experiment="experimental evidence, no additional details
recorded"
/note="N6-succinyllysine, alternate.
{ECO:0000250|UniProtKB:P08228}; propagated from
UniProtKB/Swiss-Prot (P00443.2)"
CDS 1..154
/gene="SOD1"
/gene_synonym="CU/ZN-SOD"
/coded_by="NM_001081826.3:100..564"
/db_xref="GeneID:100033855"
/db_xref="VGNC:VGNC:23442"
ORIGIN
1 malkavcvlk gdgpvhgvih feqqqeggpv vlkgfieglt kgdhgfhvhe fgdntqgctt
61 agahfnplsk khggpkdeer hvgdlgnvta dengkadvdm kdsvislsgk hsiigrtmvv
121 hekqddlgkg gneestktgn agsrlacgvi giap
//
