ID   CRUST_PANBO             Reviewed;         323 AA.
AC   Q86GF7;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Crustapain;
DE            EC=3.4.22.-;
DE   AltName: Full=NsCys;
DE   Flags: Precursor;
GN   Name=Cys {ECO:0000312|EMBL:BAC65417.1};
OS   Pandalus borealis (Northern red shrimp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Caridea;
OC   Pandaloidea; Pandalidae; Pandalus.
OX   NCBI_TaxID=6703;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAC65417.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Hepatopancreas {ECO:0000312|EMBL:BAC65417.1};
RX   PubMed=12869537; DOI=10.1093/jb/mvg102;
RA   Aoki H., Ahsan M.N., Watabe S.;
RT   "Molecular cloning and functional characterization of crustapain: a
RT   distinct cysteine proteinase with unique substrate specificity from
RT   northern shrimp Pandalus borealis.";
RL   J. Biochem. 133:799-810(2003).
CC   -!- FUNCTION: Cysteine protease which may be involved in digestion. Shows
CC       highest affinity for proline at the P2 position. Cleaves valine more
CC       efficiently than leucine and exhibits 10-fold lower affinity for
CC       phenylalanine than proline. Can cleave type I collagen.
CC       {ECO:0000269|PubMed:12869537}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=118 uM for Z-Phe-Arg-MCA (at pH 4.0)
CC         {ECO:0000269|PubMed:12869537};
CC         KM=78 uM for Z-Phe-Arg-MCA (at pH 6.0) {ECO:0000269|PubMed:12869537};
CC         KM=86 uM for Z-Phe-Arg-MCA (at pH 8.0) {ECO:0000269|PubMed:12869537};
CC         KM=98 uM for Z Pro-Arg-MCA (at pH 4.0) {ECO:0000269|PubMed:12869537};
CC         KM=65 uM for Z-Pro-Arg-MCA (at pH 6.0) {ECO:0000269|PubMed:12869537};
CC         KM=70 uM for Z-Pro-Arg-MCA (at pH 8.0) {ECO:0000269|PubMed:12869537};
CC       pH dependence:
CC         Optimum pH is 6.0. Unstable at pH values less than 5.0 and remains
CC         fully active over a wide alkaline pH range.
CC         {ECO:0000269|PubMed:12869537};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius but displays considerable
CC         activity as low as 20 degrees Celsius. Thermostable. Retains 60% of
CC         initial activity after incubation at 50 degrees Celsius for 2 hours.
CC         {ECO:0000269|PubMed:12869537};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC       ECO:0000255|PROSITE-ProRule:PRU10090}.
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; AB091669; BAC65417.1; -; mRNA.
DR   AlphaFoldDB; Q86GF7; -.
DR   SMR; Q86GF7; -.
DR   MEROPS; C01.030; -.
DR   GO; GO:0005576; C:extracellular region; IC:UniProtKB.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
DR   GO; GO:0030574; P:collagen catabolic process; IDA:UniProtKB.
DR   GO; GO:0007586; P:digestion; NAS:UniProtKB.
DR   GO; GO:0030163; P:protein catabolic process; NAS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00848; Inhibitor_I29; 1.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   1: Evidence at protein level;
KW   Collagen degradation; Digestion; Direct protein sequencing; Disulfide bond;
KW   Hydrolase; Protease; Secreted; Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..106
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:12869537"
FT                   /id="PRO_0000233915"
FT   CHAIN           107..323
FT                   /note="Crustapain"
FT                   /evidence="ECO:0000269|PubMed:12869537"
FT                   /id="PRO_0000233916"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000250|UniProtKB:P07711"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000250|UniProtKB:P07711"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000250|UniProtKB:P07711"
FT   DISULFID        127..170
FT                   /evidence="ECO:0000250|UniProtKB:P07711"
FT   DISULFID        161..203
FT                   /evidence="ECO:0000250|UniProtKB:P07711"
FT   DISULFID        262..312
FT                   /evidence="ECO:0000250|UniProtKB:P07711"
SQ   SEQUENCE   323 AA;  35525 MW;  48E083A10AB92EF0 CRC64;
     MRSLFLILLG LAAVSAIGEW ENFKTKFGKK YANSEEESHR MSVFMDKLKF IQEHNERYDK
     GEVTYWLKIN NFSDLTHEEV LATKTGMTRR RHPLSVLPKS APTTPMAADV DWRNKGAVTP
     VKDQGQCGSC WAFSAVAALE GAHFLKTGDL VSLSEQNLVD CSSSYGNQGC NGGWPYQAYQ
     YIIANRGIDT ESSYPYKAID DNCRYDAGNI GATVSSYVEP ASGDESALQH AVQNEGPVSV
     CIDAGQSSFG SYGGGVYYEP NCDSWYANHA VTAVGYGTDA NGGDYWIVKN SWGAWWGESG
     YIKMARNRDN NCAIATYSVY PVV