ID A0A060XWD1_ONCMY Unreviewed; 494 AA.
AC A0A060XWD1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 08-NOV-2023, entry version 26.
DE RecName: Full=Serpin domain-containing protein {ECO:0000259|SMART:SM00093};
GN ORFNames=GSONMT00004211001 {ECO:0000313|EMBL:CDQ81434.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ81434.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ81434.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ81434.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the serpin family.
CC {ECO:0000256|RuleBase:RU000411}.
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DR EMBL; FR905760; CDQ81434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060XWD1; -.
DR STRING; 8022.A0A060XWD1; -.
DR PaxDb; 8022-A0A060XWD1; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0051918; P:negative regulation of fibrinolysis; IEA:InterPro.
DR CDD; cd02053; serpinF2_A2AP; 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; IPR033833; Alpha2AP_serpin_dom.
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:SF20; ALPHA-2-ANTIPLASMIN; 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:UP000193380};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..494
FT /note="Serpin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001595562"
FT DOMAIN 115..454
FT /note="Serpin"
FT /evidence="ECO:0000259|SMART:SM00093"
FT REGION 35..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 54234 MW; B269BA2756969030 CRC64;
MDLRLLSLLL FCVCRQGLTN GEVSNDAPIP LVPLIPLMPS HPKEESGTSA PSTQEPQNTS
PTSYTSITHL LVTASALGGG SSEEDNQGQD GGCRAQARRP KSRQALAGAI QRLGMKLLGQ
MKTGPVQPNV IISPLSISLA LSQLALGAMN ETEELLMLHL HGDTLPCYHM SLHYFLERLR
KSDLQVAARV YLQPGFEPKP EFIHQSQDVY DSEPVTLEGM AEVNEWVERA TNGKVTDFLT
SLPPNLLLML VNAVHFKGEW KARFDPRFTS KDVFYIDDKH MVNVDMMMGP KYPLSLLIDN
DLEAQVARFP FNNQMSLLIV MPMNGQVNVS ALAAKLNISD LYNRLPRERP MQVKLPKFKL
DYSQDLQEAL TNIGMGELFS SPNLAAIAEG PLLVSSVQHK SSMEITEEGA EAAAATSLVI
SRSNPSFTLN QPFFFALMDD KTQAPIFLGV ITNPNPGAST VQSSGGSANL DKVRFPIDDK
NDKHYHHSFG GPPK
//
