ID A0A3B5QAB4_XIPMA Unreviewed; 409 AA.
AC A0A3B5QAB4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Serine protease inhibitor 2.1-like {ECO:0000313|Ensembl:ENSXMAP00000027842.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000027842.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000027842.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000027842.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the serpin family.
CC {ECO:0000256|ARBA:ARBA00009500, ECO:0000256|RuleBase:RU000411}.
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DR AlphaFoldDB; A0A3B5QAB4; -.
DR STRING; 8083.ENSXMAP00000027842; -.
DR Ensembl; ENSXMAT00000039470.1; ENSXMAP00000027842.1; ENSXMAG00000023967.1.
DR GeneTree; ENSGT00940000164899; -.
DR InParanoid; A0A3B5QAB4; -.
DR OMA; LWFNRPF; -.
DR Proteomes; UP000002852; 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 Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1.
DR Gene3D; 2.10.310.10; Serpins superfamily; 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:SF165; ALPHA-1-ANTITRYPSIN; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..409
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017445535"
FT DOMAIN 54..407
FT /note="Serpin"
FT /evidence="ECO:0000259|SMART:SM00093"
SQ SEQUENCE 409 AA; 45404 MW; 0D2177E849C50F05 CRC64;
MVSTILVLWT FLTVICTARG HQPIAQAKQA TDLSADISDD KLLLVSSANK EFAFNLYRKL
VAHPSAKGQH IFFSPISVSA ALAALSVGAR GATRQQLFHT LDFNSSQLSQ TDVNASFLKI
IGSMAFKISQ GTAVFVDNLF TPKPDFLHVL KQCYFTEGFK IDFTNPIEST NTINRYVSGM
TSGKITQLKN LDPSTVLYLL SYIYFKGIWA TPFDPKLTTL DLFRVTETIE VPVPMMRMEA
DVETYYDEAI ATSVLHLPFN NSYSMLLLLP DTMATLENKI SPAHITRWLQ RMKQRLEEYK
ISVPMFYMKT SYKLNDVLAE MGMADMFGDH ANLSGIADGQ KLVVSEVVHQ ATLDVDETGA
TAAAATGVGI SFFSHTAPEL KFNRPFIVMI TEVSAENIIF MGKIVNPNI
//