EP45_XENLA
ID EP45_XENLA Reviewed; 436 AA.
AC Q00387; B7ZSE2;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Serine protease inhibitor A6;
DE Short=Serpin A6;
DE AltName: Full=Estrogen-regulated protein EP45;
DE Flags: Precursor;
GN Name=serpina6; Synonyms=ep45;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RC TISSUE=Hepatocyte;
RX PubMed=1551912; DOI=10.1016/s0021-9258(19)50535-x;
RA Holland L.J., Suksang C., Wall A.A., Roberts L.R., Moser D.R.,
RA Bhattacharya A.;
RT "A major estrogen-regulated protein secreted from the liver of Xenopus
RT laevis is a member of the serpin superfamily. Nucleotide sequence of cDNA
RT and hormonal induction of mRNA.";
RL J. Biol. Chem. 267:7053-7059(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Not yet known.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:1551912}.
CC -!- TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:1551912}.
CC -!- INDUCTION: By estrogen. {ECO:0000269|PubMed:1551912}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; M76410; AAA49703.1; -; mRNA.
DR EMBL; BC170492; AAI70492.1; -; mRNA.
DR EMBL; BC170494; AAI70494.1; -; mRNA.
DR PIR; A42440; A42440.
DR RefSeq; NP_001079103.1; NM_001085634.1.
DR AlphaFoldDB; Q00387; -.
DR SMR; Q00387; -.
DR ABCD; Q00387; 1 sequenced antibody.
DR GeneID; 373636; -.
DR KEGG; xla:373636; -.
DR CTD; 373636; -.
DR Xenbase; XB-GENE-6252882; serpina6.L.
DR OMA; IMFLNIS; -.
DR OrthoDB; 1124079at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 373636; Expressed in liver and 3 other tissues.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 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; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..436
FT /note="Serine protease inhibitor A6"
FT /id="PRO_0000032536"
FT REGION 26..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 297
FT /note="V -> F (in Ref. 1; AAA49703)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 49523 MW; A0A229D415FAE6C1 CRC64;
MHLLVYLSLF FALALASVTE ISLDNKHRHR HEQQGHHDSA KHGHQKDKQQ QEQIKNDEGK
LTKEEKILSE ENSDFSVNLF NQLSTESKRS PRKNIFFSPI SISAAFYMLA LGAKSETHQQ
ILKGLSFNKK KLSESQVHEA FKRLIEDSNN PMKAHQFTIG NALFVEQTVN ILKGFEENVK
HYYQAGVFPM NFKDPDNAKK QLNNYVKDKT HGVIQEMIRE LDSNTEMVLV NYVLYKGEWA
NNFNPTLTQK SLFSVDKNTN VTVQMMNRLG LYRTYQDDDC KIIELPYKND TAMLLVVPQL
GKIQELVLTS KLINHWYESL ATSIVDLYMP TFSISGKVVL KDTLRKMGIS DIFTDKADLT
GISEQIKLKV SMASHNAVLN VNEFGTEAVG ATSAQASPTK LFPPFLIDSP FLVMIYSRTL
GSQLFMGKVM DPTNAQ