ID A0A2Y9QZB0_TRIMA Unreviewed; 404 AA.
AC A0A2Y9QZB0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Protein Z-dependent protease inhibitor {ECO:0000313|RefSeq:XP_023587427.1};
GN Name=LOC101344714 {ECO:0000313|RefSeq:XP_023587427.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023587427.1};
RN [1] {ECO:0000313|RefSeq:XP_023587427.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the serpin family.
CC {ECO:0000256|RuleBase:RU000411}.
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 RefSeq; XP_023587427.1; XM_023731659.1.
DR AlphaFoldDB; A0A2Y9QZB0; -.
DR STRING; 127582.A0A2Y9QZB0; -.
DR KEGG; tmu:101344714; -.
DR InParanoid; A0A2Y9QZB0; -.
DR OrthoDB; 3218836at2759; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0007596; P:blood coagulation; IEA:InterPro.
DR CDD; cd02055; serpinA10_PZI; 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; IPR033835; PZI_serpin_dom.
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:SF191; PROTEIN Z-DEPENDENT PROTEASE INHIBITOR; 1.
DR PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR Pfam; PF00079; Serpin; 1.
DR PRINTS; PR00780; LEUSERPINII.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; Serpins; 1.
PE 3: Inferred from homology;
KW Protease inhibitor {ECO:0000313|RefSeq:XP_023587427.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..404
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015997732"
FT DOMAIN 74..404
FT /note="Serpin"
FT /evidence="ECO:0000259|SMART:SM00093"
FT REGION 28..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 404 AA; 45974 MW; 5088A5E4155A10E9 CRC64;
MKLVLRLLFL FLLAEVWLVP GFAPGTQPPE AEAGPGTLRT LAPQNQPPEE KKEEEPWLVA
SRQELSQETS NFGFSLLRKI SVKHEGNVVF SPLSLSFAMA TLVLGAAGPT RTQILSGLGL
QALNGTQPAL LPALFGHLRE TLSRNWELGL TQGSLAFIHK DFDVKETFLN LSKRYFDTAC
VPMNFRNASQ AKGLMNQYIS KETQGRIPKL FDEINPETKV ILVDYILFKG QWLTPFDPVF
TEADTFRLDK YKAVKVPMMY RAGNFASTFD KNFRCHVLKL PYQGNATMLV VLMQKMGDHL
ALEDYLTTEL VETWLRNMKT RKMEVFLPKF KLDQKYEMHE LLKQMGIRRI FSSWADLSEL
SVTTRNLKVS KVLQRAMIEV DEKGTEAFQD PIQITTFHLI VMST
//
