ID   SPI_CYACP               Reviewed;         377 AA.
AC   Q6J201;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Serine protease inhibitor {ECO:0000312|EMBL:AAT35220.1};
DE   AltName: Full=Jellypin {ECO:0000303|PubMed:15362859};
DE            Short=JP {ECO:0000303|PubMed:15362859};
DE   Flags: Precursor;
OS   Cyanea capillata (Lion's mane jellyfish) (Cyanea arctica).
OC   Eukaryota; Metazoa; Cnidaria; Scyphozoa; Semaeostomeae; Cyaneidae; Cyanea.
OX   NCBI_TaxID=27804;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAT35220.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, REACTIVE SITE FOR CHYMOTRYPSIN, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15362859; DOI=10.1021/bi049020u;
RA   Cole E.B., Miller D., Rometo D., Greenberg R.M., Bromme D., Cataltepe S.,
RA   Pak S.C., Mills D.R., Silverman G.A., Luke C.J.;
RT   "Identification and activity of a lower eukaryotic serine proteinase
RT   inhibitor (serpin) from Cyanea capillata: analysis of a jellyfish serpin,
RT   jellypin.";
RL   Biochemistry 43:11750-11759(2004).
CC   -!- FUNCTION: Inhibitor of serine proteases. Inhibits chymotrypsin,
CC       cathepsin G and human neutrophil elastase.
CC       {ECO:0000269|PubMed:15362859}.
CC   -!- DOMAIN: The reactive center loop (RCL) extends out from the body of the
CC       protein and directs binding to the target protease. The protease
CC       cleaves the serpin at the reactive site within the RCL, establishing a
CC       covalent linkage between the carboxyl group of the serpin reactive site
CC       and the serine hydroxyl of the protease. The resulting inactive serpin-
CC       protease complex is highly stable (By similarity).
CC       {ECO:0000250|UniProtKB:P01009}.
CC   -!- MISCELLANEOUS: Possesses several potential secondary cleavage sites.
CC       {ECO:0000269|PubMed:15362859}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000255}.
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; AY605047; AAT35220.1; -; mRNA.
DR   AlphaFoldDB; Q6J201; -.
DR   SMR; Q6J201; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR   Gene3D; 2.30.39.10; -; 1.
DR   Gene3D; 3.30.497.10; -; 1.
DR   InterPro; IPR015557; Serpin_B1.
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   PANTHER; PTHR11461:SF180; PTHR11461:SF180; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; SSF56574; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Protease inhibitor; Serine protease inhibitor; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..377
FT                   /note="Serine protease inhibitor"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000389520"
FT   REGION          328..349
FT                   /note="RCL"
FT                   /evidence="ECO:0000255"
FT   SITE            342..343
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000269|PubMed:15362859"
FT   CARBOHYD        301
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   377 AA;  41052 MW;  B968F84199888DAE CRC64;
     MAALQAAVSS QLAISFFSSL IVPGAEKNVV CSPLSISSAL ALVAAGSRGK TLKEIADALN
     WREDADGLAK ALLAEAEKAA QNCDASCPVK TANNVWVDNE FKILDSYRDL LKSFAVNVGK
     ADFKKHSSDE TIKINSWIED HTNKKIRDFF PPGELSEATK AVLVNALYFK GKWAEPFDME
     STRDDTFHVS NSKEVQVKMM YHSAELKYFM DENSKCDLVE LPYSSKAFSM MLIVPHEVEG
     LSAVQSSLSL SQVSGWISNV QSAAPQTVDV FLPRFKVSQK VNMKDNLKSL GINDMFSMQA
     NLSGIAGSHD LFVSSAIHQA VIEVNEEGTE AAAATGFGVN FMSMPMQVRA DKPFLFLIIS
     NVTKSILFIG KIANPAA