ID   A0A3P8SDK2_AMPPE        Unreviewed;       463 AA.
AC   A0A3P8SDK2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Serpin B6 {ECO:0000256|ARBA:ARBA00039202};
OS   Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000010165.1, ECO:0000313|Proteomes:UP000265080};
RN   [1] {ECO:0000313|Ensembl:ENSAPEP00000010165.1, ECO:0000313|Proteomes:UP000265080}
RP   NUCLEOTIDE SEQUENCE.
RA   Lehmann R.;
RT   "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT   of the orange clownfish Amphiprion percula.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPEP00000010165.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBUNIT: Forms a complex with the monomeric form of beta-tryptase.
CC       {ECO:0000256|ARBA:ARBA00038828}.
CC   -!- SIMILARITY: Belongs to the serpin family.
CC       {ECO:0000256|RuleBase:RU000411}.
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DR   AlphaFoldDB; A0A3P8SDK2; -.
DR   STRING; 161767.ENSAPEP00000010165; -.
DR   Ensembl; ENSAPET00000010441.1; ENSAPEP00000010165.1; ENSAPEG00000007308.1.
DR   GeneTree; ENSGT00940000154835; -.
DR   OMA; AWTKPEC; -.
DR   Proteomes; UP000265080; Chromosome 22.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   CDD; cd19956; serpinB; 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; 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; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   PANTHER; PTHR11461:SF204; SERPIN B6; 1.
DR   Pfam; PF00079; Serpin; 2.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265080}.
FT   DOMAIN          17..462
FT                   /note="Serpin"
FT                   /evidence="ECO:0000259|SMART:SM00093"
FT   REGION          70..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   463 AA;  51828 MW;  5C818398C2DFD660 CRC64;
     MASEGNPVPE AITKFCLSLL QKLSEDDSSA NLFLSPFSIS TALAMVMLGT AGETATQMSK
     VLCFTEQSDQ AGGQQTQLSP MQQLHEERQE RMQMQPQVQT QQSSRLPPYL LKILKDKTDD
     ANKTDEDANK TDDVSSNDFQ PQCELNKPVD VHADFGKLLS ELNKNDAPYA LSLANRLYGE
     KSYQFIEEFL ADIKKEYKAE LESVDFKSSA EEVRVNINEW VEKQTQGKIK DLLGKNAVDG
     LTRLVLVNAI YFKGNWNQKF NEKDTADAAF KINKNDTKEV KMMRLTSTFP VAVIPELNSR
     VLEMPYKGKD LSMLILLPDQ IEDDSTGLEK LESKLTYEKF VEWTSPVMKN EIEVQVSLPR
     FKLEEKYDMK DVLVSMGMVD AFDTAKSDFS GMSSANDLVL SKVVHKAFVD VNEEGTEAAA
     ATGGVVSTLS LPEMFTADHP FLFFIRHNPS STILFAGKFC SPM
//