ID   SPB5_XENLA              Reviewed;         383 AA.
AC   Q6GLQ1;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Serpin B5;
GN   Name=serpinb5;
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 [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May not exhibit serine protease inhibitory activity.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC074408; AAH74408.1; -; mRNA.
DR   RefSeq; NP_001086270.1; NM_001092801.1.
DR   RefSeq; XP_018124197.1; XM_018268708.1.
DR   RefSeq; XP_018124198.1; XM_018268709.1.
DR   AlphaFoldDB; Q6GLQ1; -.
DR   SMR; Q6GLQ1; -.
DR   MEROPS; I04.980; -.
DR   DNASU; 444699; -.
DR   GeneID; 444699; -.
DR   KEGG; xla:444699; -.
DR   CTD; 444699; -.
DR   Xenbase; XB-GENE-5803019; serpinb5.S.
DR   OMA; FSEMCET; -.
DR   OrthoDB; 1124079at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 444699; Expressed in zone of skin and 9 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   CDD; cd02057; serpinB5_maspin; 1.
DR   Gene3D; 2.30.39.10; -; 1.
DR   Gene3D; 3.30.497.10; -; 1.
DR   InterPro; IPR000240; Serpin_B9/Maspin.
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   InterPro; IPR033836; SERPINB5_serpin_dom.
DR   PANTHER; PTHR11461; PTHR11461; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   PRINTS; PR00676; MASPIN.
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.
FT   CHAIN           1..383
FT                   /note="Serpin B5"
FT                   /id="PRO_0000372429"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   383 AA;  43417 MW;  AAA66341312A1893 CRC64;
     MDALRLANTG LAVDIFKKLC EKSATDNFVF SPICISTSLA LLHRGSQGNT ASELQKVLHF
     EKVKDSDFGF QLLSSDISKV ISIYSLKLLK RVYVDNSIEC KKDFINSTKK PYPLELETID
     IKSRPEEARC QINSSVKELT DGNFEAVLNE GSCDEKTKII MLGAASFKGN WVYKFNESET
     KEMDFHINKK ETKPVQMMHL EARLSIGYIN ELKTMVLELP FTSKHLSILI LLPKDIEDDS
     TGLKKLEQDM TFEKYAQWTN PSMMANSKVK VYLPKFKLES SFDLKDMLKS LGINDAFNEE
     ASDFSGMTES KDTSISQAIH KACIEVNEDG TEAPDVTMER RLMNKEEFCA DRPFIFILRH
     NKTRTIIMFG RYCGPCEASS TAD