ESM1_DROSI
ID ESM1_DROSI Reviewed; 156 AA.
AC B4QW11;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Enhancer of split M1 protein {ECO:0000303|PubMed:15537803};
DE Short=E(spl)m1 {ECO:0000303|PubMed:15537803};
DE AltName: Full=Kazal-type protease inhibitor m1 {ECO:0000250|UniProtKB:O97176};
DE Flags: Precursor;
GN Name=Kaz-m1 {ECO:0000250|UniProtKB:O97176}; Synonyms=m1; ORFNames=GD21260;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAV59245.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=sim6 {ECO:0000269|PubMed:15537803};
RX PubMed=15537803; DOI=10.1093/molbev/msi046;
RA Macdonald S.J., Long A.D.;
RT "Identifying signatures of selection at the enhancer of split neurogenic
RT gene complex in Drosophila.";
RL Mol. Biol. Evol. 22:607-619(2005).
RN [2] {ECO:0000312|EMBL:EDX14510.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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DR EMBL; AY779922; AAV59245.1; -; Genomic_DNA.
DR EMBL; CM000364; EDX14510.1; -; Genomic_DNA.
DR RefSeq; XP_002105007.1; XM_002104971.2.
DR AlphaFoldDB; B4QW11; -.
DR STRING; 7240.B4QW11; -.
DR EnsemblMetazoa; FBtr0221170; FBpp0219662; FBgn0082722.
DR GeneID; 6729701; -.
DR HOGENOM; CLU_1604439_0_0_1; -.
DR OMA; CSMIYQP; -.
DR PhylomeDB; B4QW11; -.
DR Proteomes; UP000000304; Chromosome 3r.
DR Bgee; FBgn0082722; Expressed in embryo and 3 other tissues.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR Pfam; PF07648; Kazal_2; 2.
DR SMART; SM00280; KAZAL; 2.
DR SUPFAM; SSF100895; SSF100895; 1.
DR PROSITE; PS51465; KAZAL_2; 2.
PE 3: Inferred from homology;
KW Disulfide bond; Protease inhibitor; Reference proteome; Repeat;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..156
FT /note="Enhancer of split M1 protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000423185"
FT DOMAIN 23..81
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 96..156
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 35..36
FT /note="Reactive bond"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 108..109
FT /note="Reactive bond"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 29..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 33..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 102..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 106..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 114..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ SEQUENCE 156 AA; 17325 MW; 6892B5E1C89F6D92 CRC64;
MMSQTLTLCC LGLVACVYGN TVSTNDTACP TFCPSIYKPV CGTDGQNFKE FASTCNLLSH
NCRRERNSVQ AYAATDAAWC SSEFVENLHE KLGNFKLEVK ECFKPCSMIY QPVCITNGKY
RAELANSCLL ENFNCALQVS GAQPAELFRL LREEKC
