ID B3S279_TRIAD Unreviewed; 356 AA.
AC B3S279;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=Serpin domain-containing protein {ECO:0000259|SMART:SM00093};
GN ORFNames=TRIADDRAFT_63332 {ECO:0000313|EMBL:EDV23068.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV23068.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV23068.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV23068.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- SIMILARITY: Belongs to the serpin family.
CC {ECO:0000256|RuleBase:RU000411}.
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DR EMBL; DS985247; EDV23068.1; -; Genomic_DNA.
DR RefSeq; XP_002113978.1; XM_002113942.1.
DR AlphaFoldDB; B3S279; -.
DR STRING; 10228.B3S279; -.
DR MEROPS; I04.073; -.
DR EnsemblMetazoa; TriadT63332; TriadP63332; TriadG63332.
DR GeneID; 6755508; -.
DR KEGG; tad:TRIADDRAFT_63332; -.
DR CTD; 6755508; -.
DR eggNOG; KOG2392; Eukaryota.
DR HOGENOM; CLU_023330_0_1_1; -.
DR InParanoid; B3S279; -.
DR OMA; FKMEERY; -.
DR OrthoDB; 3218836at2759; -.
DR PhylomeDB; B3S279; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd19590; serpin_thermopin-like; 1.
DR Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1.
DR InterPro; IPR023795; Serpin_CS.
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:SF211; ACCESSORY GLAND PROTEIN ACP76A-RELATED; 1.
DR PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; Serpins; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT DOMAIN 1..349
FT /note="Serpin"
FT /evidence="ECO:0000259|SMART:SM00093"
SQ SEQUENCE 356 AA; 40155 MW; F8B107EE8DA290C3 CRC64;
MPPKQDVTLS PLSIFTCLAM TYGGAQGKTA KEMQSVLHIE SDNIHQALQI ILRAIIGSDN
QSGHTFKAAN RLFFSTNYSL LPQYLDLTKT FYNAQPQSVN FSHAAEAAGI INTWVENQTA
KKIKDLIPAS GINPLTRLIL VNALYFKGNW SDKFDKNLTQ KMDFKIDNSN KVQVHMMSKT
KKLNYMADMD IGFQMVELPY AHDSLSMFVI LPRDIDGINS LCKHINSANL QQWIVNLSLP
RFKMTYQTAL SDLLRNLGMI DAFDNKNADF SKMCSDNDLY ITEIFHKVFI EVNERGTEAA
AATGAVARYK TRSKRPPLIK VMTVDHPFVF MMYHKSSGST LFLGKMYNPA INPSVR
//
