ID A0A423U351_PENVA Unreviewed; 432 AA.
AC A0A423U351;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 08-NOV-2023, entry version 13.
DE SubName: Full=Serine proteinase inhibitor {ECO:0000313|EMBL:ROT83126.1};
GN ORFNames=C7M84_023696 {ECO:0000313|EMBL:ROT83126.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT83126.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBL:ROT83126.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT83126.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT83126.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT83126.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molting mechanism and breeding impact on genome.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the serpin family.
CC {ECO:0000256|RuleBase:RU000411}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROT83126.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QCYY01000733; ROT83126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423U351; -.
DR EnsemblMetazoa; XM_027350654.1; XP_027206455.1; LOC113799948.
DR EnsemblMetazoa; XM_027350655.1; XP_027206456.1; LOC113799948.
DR OrthoDB; 3020821at2759; -.
DR Proteomes; UP000283509; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
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:SF278; SERINE PROTEASE INHIBITOR 88EA; 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 Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..432
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019384162"
FT DOMAIN 46..426
FT /note="Serpin"
FT /evidence="ECO:0000259|SMART:SM00093"
SQ SEQUENCE 432 AA; 48039 MW; 3DF124FAA4F4DDC5 CRC64;
MRWILAAVVV LGASVWEATS QCLTDEDRIK ILGVNQELNE VVDFGLELYK ELELGQATSY
LATGRNLFFS PYSVWSALVL AYFGSGGTTE AELQKALGVV DKINILTKMR ALELTYDLRR
STGSSYIFNV ANRFYIDAAS PVRKCVKNIL FKEIAETDFR NTFVAANDIN EFVSETTQGN
IPRLLEESDL RDAQMVLVNA AFFKGIWKYS FLSNDTFLAP FRADPSLSFQ GGAGTPPNGT
GMVSMMNQTA SFKYADSKDL EAQLLELPYE GGAMSMFLML PNEEGRSGFA RTVASFSSAA
LSKAMRTMKP ETVNLQLPRF NMSVELIDEL EAALKNLGIR NVFDPEHADF SAFAPTPRMS
VSKTVHKAFI EVNEEGSEAA AATVLAVNIR TRPKPPLSFV CDRPFIFFIY DNDTENILFL
GVFRNHKEAL DY
//
