PCPI_SABMA
ID PCPI_SABMA Reviewed; 165 AA.
AC P84875; A0PDV9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Carboxypeptidase inhibitor SmCI;
OS Sabellastarte magnifica (Feather duster).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Sedentaria; Canalipalpata; Sabellida; Sabellidae; Sabellastarte.
OX NCBI_TaxID=389514;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-22 AND 29-165, FUNCTION,
RP MASS SPECTROMETRY, GLYCOSYLATION AT ASN-23, AND DISULFIDE BONDS.
RA Alonso del Rivero M., Trejo S., Rodriguez de la Vega M., Delfin J.,
RA Diaz J., Gonzalez Y., Canals F., Chavez M.A., Aviles F.X.;
RT "A novel bifunctional inhibitor of metallo carboxypeptidase and serine
RT proteinase isolated from the annelid Sabellastarte magnifica. Isolation,
RT characterization and cDNA cloning.";
RL Submitted (JUN-2006) to UniProtKB.
CC -!- FUNCTION: Potent inhibitor of pancreatic carboxypeptidase A with a Ki
CC of 27 nM, and of the serine proteases trypsin, chymotrypsin and
CC pancreatic elastase, with Ki values of 6.9 nM, 1.83 nM and 4 nM,
CC respectively. Does not inhibit cysteine and aspartic proteases.
CC {ECO:0000269|Ref.1}.
CC -!- INTERACTION:
CC P84875; Q9UI42-1: CPA4; Xeno; NbExp=3; IntAct=EBI-16060264, EBI-16060275;
CC -!- TISSUE SPECIFICITY: Expressed in the tentacle crown. Not detected in
CC annelid body. {ECO:0000269|Ref.1}.
CC -!- PTM: Contains 9 disulfide bonds. {ECO:0000269|Ref.1}.
CC -!- MASS SPECTROMETRY: Mass=19700; Method=MALDI;
CC Evidence={ECO:0000269|Ref.1};
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DR EMBL; AM283480; CAK55547.1; -; Genomic_DNA.
DR PDB; 4BD9; X-ray; 2.20 A; B=1-165.
DR PDBsum; 4BD9; -.
DR AlphaFoldDB; P84875; -.
DR SMR; P84875; -.
DR DIP; DIP-60557N; -.
DR IntAct; P84875; 3.
DR MEROPS; I02.064; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00109; KU; 3.
DR Gene3D; 4.10.410.10; -; 3.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR008296; TFPI-like.
DR Pfam; PF00014; Kunitz_BPTI; 3.
DR PIRSF; PIRSF001620; TFPI; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 3.
DR SUPFAM; SSF57362; SSF57362; 3.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 3.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW Repeat; Serine protease inhibitor.
FT CHAIN 1..165
FT /note="Carboxypeptidase inhibitor SmCI"
FT /id="PRO_0000271256"
FT DOMAIN 4..54
FT /note="BPTI/Kunitz inhibitor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 56..106
FT /note="BPTI/Kunitz inhibitor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 115..165
FT /note="BPTI/Kunitz inhibitor 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.1"
FT DISULFID 4..54
FT /evidence="ECO:0000250|UniProtKB:P02760,
FT ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 13..37
FT /evidence="ECO:0000250|UniProtKB:P02760,
FT ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 29..50
FT /evidence="ECO:0000250|UniProtKB:P02760,
FT ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 56..106
FT /evidence="ECO:0000250|UniProtKB:P02760,
FT ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 65..89
FT /evidence="ECO:0000250|UniProtKB:P02760,
FT ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 81..102
FT /evidence="ECO:0000250|UniProtKB:P02760,
FT ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 115..165
FT /evidence="ECO:0000250|UniProtKB:P10646,
FT ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 124..148
FT /evidence="ECO:0000250|UniProtKB:P10646,
FT ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 140..161
FT /evidence="ECO:0000250|UniProtKB:P10646,
FT ECO:0000255|PROSITE-ProRule:PRU00031"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:4BD9"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:4BD9"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:4BD9"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:4BD9"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:4BD9"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:4BD9"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:4BD9"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:4BD9"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:4BD9"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:4BD9"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:4BD9"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:4BD9"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:4BD9"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:4BD9"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:4BD9"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:4BD9"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:4BD9"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:4BD9"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:4BD9"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:4BD9"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:4BD9"
FT HELIX 158..164
FT /evidence="ECO:0007829|PDB:4BD9"
SQ SEQUENCE 165 AA; 18650 MW; 74BE24DFBC745246 CRC64;
ISVCDLPADR GQCTAYIPQW FFNKTTEDCE KFVYGGCQGN ANRFETKDDC IANCGCNLPS
KVGPCRVSAR MWFHNPETEK CEVFIYGGCH GNANRFATET ECQEVCDRYQ KPGFCYQPSE
TGPCKGSFPR YYYDYEDGEC KEFIYGGCEG NANNFETKES CENAC
