ID A0A0M5JD07_DROBS Unreviewed; 624 AA.
AC A0A0M5JD07;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Spn100A {ECO:0000313|EMBL:ALC47606.1};
GN ORFNames=Dbus_chr3Rg2356 {ECO:0000313|EMBL:ALC47606.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC47606.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC47606.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC47606.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the serpin family.
CC {ECO:0000256|RuleBase:RU000411}.
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DR EMBL; CP012526; ALC47606.1; -; Genomic_DNA.
DR RefSeq; XP_017845402.1; XM_017989913.1.
DR AlphaFoldDB; A0A0M5JD07; -.
DR STRING; 30019.A0A0M5JD07; -.
DR GeneID; 108601935; -.
DR OMA; EFFFMTN; -.
DR OrthoDB; 3672676at2759; -.
DR Proteomes; UP000494163; Chromosome 3r sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00172; serpin; 1.
DR Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 2.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR PANTHER; PTHR11461:SF292; SERPIN 100A; 1.
DR Pfam; PF00079; Serpin; 2.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; Serpins; 1.
PE 3: Inferred from homology;
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000494163};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..624
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005803702"
FT DOMAIN 41..606
FT /note="Serpin"
FT /evidence="ECO:0000259|SMART:SM00093"
FT REGION 246..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 624 AA; 70134 MW; B7BB515F26722E26 CRC64;
MKTVVLLLLL PLLVSALPKL EPKKDELPLN FASEASQLIA TQLLKHNKDI DANQVHSPLG
VAAILAVLAE AAEGETYAEF GKVFDFPQQR SAVRAAFERI LGSYQNRDAA VPLPSFQTWF
YVYRNHSVRE EYKQLLQRHY YVEVKDINRQ DYDWSEPNTS LTLEGSALSS ESTESSNGKD
VIGFETLKRI NVDDIEASPA AAAATDNYGE EVLNKQASKF DREVDDKQYV EKPVALAEVT
EAVEKLEKPA ELMPNKEEEN PAEKQQNKRS DDAQMPAVEE NETVQEDEKL RKQLNEPLTA
NEPEKVRLPL QKLENAVKSM VKEGADEIMI ALESHLSEVA RAYAGRSLFR QDDIASALSA
NSITGRQLDS KSKMLLFNGL YYRGSWAQPF YQLRDGSDEF FFMTNEDAVK TAMMHTRGQF
NVAELPHLKA RVLSLPYEQA KYALHIVLPN DPEGLTDVIA KLQPSDYKYA REHVQLKQLH
VILPKFQVEE TSRSEAMLKQ LGLKRLFSRT EAQLSLLSDD EDVHVDEIVQ FVNVRVDEGG
SGANSLSAAT MQARTPAAET TETLPVPEPE PEPAGVERFE VNHPFAYFIM DCEQQFVLAS
GKVYAPEFKD ELPPVSIEIE LEQA
//
