ID   PCSK6_HUMAN             Reviewed;         969 AA.
AC   P29122; Q15099; Q15100; Q9UEG7; Q9UEJ1; Q9UEJ2; Q9UEJ7; Q9UEJ8; Q9UEJ9;
AC   Q9Y4G9; Q9Y4H0; Q9Y4H1;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   27-MAR-2024, entry version 219.
DE   RecName: Full=Proprotein convertase subtilisin/kexin type 6;
DE            EC=3.4.21.-;
DE   AltName: Full=Paired basic amino acid cleaving enzyme 4;
DE   AltName: Full=Subtilisin-like proprotein convertase 4;
DE            Short=SPC4;
DE   AltName: Full=Subtilisin/kexin-like protease PACE4;
DE   Flags: Precursor;
GN   Name=PCSK6; Synonyms=PACE4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PACE4A-I AND PACE4B).
RC   TISSUE=Hepatoma, and Kidney;
RX   PubMed=1741956; DOI=10.1089/dna.1991.10.757;
RA   Kiefer M.C., Tucker J.E., Joh R., Landsberg K.E., Saltman D., Barr P.J.;
RT   "Identification of a second human subtilisin-like protease gene in the
RT   fes/fps region of chromosome 15.";
RL   DNA Cell Biol. 10:757-769(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PACE4C AND PACE4D).
RC   TISSUE=Placenta;
RX   PubMed=8179631; DOI=10.1006/bbrc.1994.1541;
RA   Tsuji A., Higashine K., Hine C., Mori K., Tamai Y., Nagamune H.,
RA   Matsuda Y.;
RT   "Identification of novel cDNAs encoding human kexin-like protease, PACE4
RT   isoforms.";
RL   Biochem. Biophys. Res. Commun. 200:943-950(1994).
RN   [3]
RP   ERRATUM OF PUBMED:8179631.
RX   PubMed=7980617; DOI=10.1006/bbrc.1994.2616;
RA   Tsuji A., Higashine K., Hine C., Mori K., Tamai Y., Nagamune H.,
RA   Matsuda Y.;
RL   Biochem. Biophys. Res. Commun. 204:1381-1382(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE (ISOFORM PACE4A-II).
RC   TISSUE=Placenta;
RA   Mori K., Imamaki A., Kii S., Nagamune H., Nagahama M., Tsuji A.,
RA   Matsuda Y.;
RT   "Identification of a novel PACE4 isoform, PACE4E.";
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PACE4E-I AND PACE4E-II).
RC   TISSUE=Cerebellum;
RX   PubMed=9192737; DOI=10.1093/oxfordjournals.jbchem.a021677;
RA   Mori K., Kii S., Tsuji A., Nagahama M., Imamaki A., Hayashi K.,
RA   Akamatsu T., Nagamune H., Matsuda Y.;
RT   "A novel human PACE4 isoform, PACE4E is an active processing protease
RT   containing a hydrophobic cluster at the carboxy terminus.";
RL   J. Biochem. 121:941-948(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS PACE4A-I; PACE4A-II; PACE4CS;
RP   PACE4D; PACE4E-I AND PACE4E-II).
RX   PubMed=9378725; DOI=10.1093/oxfordjournals.jbchem.a021772;
RA   Tsuji A., Hine C., Tamai Y., Yonemoto K., Mori K., Yoshida S., Bando M.,
RA   Sakai E., Mori K., Akamatsu T., Matsuda Y.;
RT   "Genomic organization and alternative splicing of human PACE4 (SPC4),
RT   kexin-like processing endoprotease.";
RL   J. Biochem. 122:438-452(1997).
RN   [7]
RP   ALTERNATIVE SPLICING (ISOFORM PACE4CS).
RX   PubMed=8906861; DOI=10.1016/0014-5793(96)01059-9;
RA   Zhong M., Benjannet S., Lazure C., Munzer S., Seidah N.G.;
RT   "Functional analysis of human PACE4-A and PACE4-C isoforms: identification
RT   of a new PACE4-CS isoform.";
RL   FEBS Lett. 396:31-36(1996).
RN   [8]
RP   CHARACTERIZATION.
RX   PubMed=10215603; DOI=10.1042/bj3390639;
RA   Sucic J.F., Moehring J.M., Inocencio N.M., Luchini J.W., Moehring T.J.;
RT   "Endoprotease PACE4 is Ca2+-dependent and temperature-sensitive and can
RT   partly rescue the phenotype of a furin-deficient cell strain.";
RL   Biochem. J. 339:639-647(1999).
RN   [9]
RP   PROTEOLYTIC PROCESSING.
RX   PubMed=9738469; DOI=10.1016/s0014-5793(98)00970-3;
RA   Nagahama M., Taniguchi T., Hashimoto E., Imamaki A., Mori K., Tsuji A.,
RA   Matsuda Y.;
RT   "Biosynthetic processing and quaternary interactions of proprotein
RT   convertase SPC4 (PACE4).";
RL   FEBS Lett. 434:155-159(1998).
RN   [10]
RP   INTERACTION WITH RCN3.
RX   PubMed=16433634; DOI=10.1042/bj20051524;
RA   Tsuji A., Kikuchi Y., Sato Y., Koide S., Yuasa K., Nagahama M., Matsuda Y.;
RT   "A proteomic approach reveals transient association of reticulocalbin-3, a
RT   novel member of the CREC family, with the precursor of subtilisin-like
RT   proprotein convertase, PACE4.";
RL   Biochem. J. 396:51-59(2006).
CC   -!- FUNCTION: Serine endoprotease that processes various proproteins by
CC       cleavage at paired basic amino acids, recognizing the RXXX[KR]R
CC       consensus motif. Likely functions in the constitutive secretory
CC       pathway, with unique restricted distribution in both neuroendocrine and
CC       non-neuroendocrine tissues.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC   -!- SUBUNIT: The PACE4A-I precursor protein seems to exist in the reticulum
CC       endoplasmic as both a monomer and a dimer-sized complex whereas mature
CC       PACE4A-I exists only as a monomer, suggesting that propeptide cleavage
CC       affects its tertiary or quaternary structure. Interacts (immature form
CC       including the propeptide) with RCN3; probably involved in the
CC       maturation and the secretion of PCSK6 (PubMed:16433634).
CC       {ECO:0000269|PubMed:16433634}.
CC   -!- INTERACTION:
CC       P29122; Q92824-2: PCSK5; NbExp=3; IntAct=EBI-2683528, EBI-11956269;
CC       P29122; Q8N8Z8: ZNF441; NbExp=3; IntAct=EBI-2683528, EBI-17216366;
CC   -!- SUBCELLULAR LOCATION: [Isoform PACE4A-I]: Secreted.
CC   -!- SUBCELLULAR LOCATION: [Isoform PACE4A-II]: Secreted.
CC   -!- SUBCELLULAR LOCATION: [Isoform PACE4C]: Endoplasmic reticulum. Note=Not
CC       secreted, remains probably in zymogen form in endoplasmic reticulum.
CC   -!- SUBCELLULAR LOCATION: [Isoform PACE4CS]: Endoplasmic reticulum.
CC       Note=Not secreted, remains probably in zymogen form in endoplasmic
CC       reticulum.
CC   -!- SUBCELLULAR LOCATION: [Isoform PACE4E-I]: Endomembrane system;
CC       Peripheral membrane protein. Note=Retained intracellularly probably
CC       through a hydrophobic cluster in their C-terminus.
CC   -!- SUBCELLULAR LOCATION: [Isoform PACE4E-II]: Endomembrane system;
CC       Peripheral membrane protein. Note=Retained intracellularly probably
CC       through a hydrophobic cluster in their C-terminus.
CC   -!- SUBCELLULAR LOCATION: [Isoform PACE4B]: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC       Name=PACE4A-I; Synonyms=PACE4;
CC         IsoId=P29122-1; Sequence=Displayed;
CC       Name=PACE4A-II;
CC         IsoId=P29122-2; Sequence=VSP_005436;
CC       Name=PACE4B; Synonyms=PACE4.1;
CC         IsoId=P29122-3; Sequence=VSP_005428, VSP_005429;
CC       Name=PACE4C;
CC         IsoId=P29122-4; Sequence=VSP_005432, VSP_005433;
CC       Name=PACE4CS;
CC         IsoId=P29122-5; Sequence=VSP_005430, VSP_005431;
CC       Name=PACE4D;
CC         IsoId=P29122-6; Sequence=VSP_005427, VSP_005434, VSP_005435;
CC       Name=PACE4E-I;
CC         IsoId=P29122-7; Sequence=VSP_005437;
CC       Name=PACE4E-II;
CC         IsoId=P29122-8; Sequence=VSP_005436, VSP_005437;
CC   -!- TISSUE SPECIFICITY: Each PACE4 isoform exhibits a unique restricted
CC       distribution. Isoform PACE4A-I is expressed in heart, brain, placenta,
CC       lung, skeletal muscle, kidney, pancreas, but at comparatively higher
CC       levels in the liver. Isoform PACE4A-II is at least expressed in
CC       placenta. Isoform PACE4B was only found in the embryonic kidney cell
CC       line from which it was isolated. Isoform PACE4C and isoform PACE4D are
CC       expressed in placenta. Isoform PACE4E-I is expressed in cerebellum,
CC       placenta and pituitary. Isoform PACE4E-II is at least present in
CC       cerebellum.
CC   -!- DOMAIN: The propeptide domain acts as an intramolecular chaperone
CC       assisting the folding of the zymogen within the endoplasmic reticulum.
CC       Isoform PACE4D lacks the propeptide domain.
CC   -!- MISCELLANEOUS: [Isoform PACE4B]: Probably enzymatically inactive.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform PACE4C]: Probably enzymatically inactive.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform PACE4CS]: Probably enzymatically inactive.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform PACE4D]: Probably enzymatically inactive.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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; M80482; AAA59998.1; -; mRNA.
DR   EMBL; AB001914; BAA21620.1; -; Genomic_DNA.
DR   EMBL; AB001914; BAA21621.1; -; Genomic_DNA.
DR   EMBL; AB001914; BAA21622.1; -; Genomic_DNA.
DR   EMBL; AB001914; BAA21623.1; -; Genomic_DNA.
DR   EMBL; AB001914; BAA21624.1; -; Genomic_DNA.
DR   EMBL; AB001914; BAA21625.1; -; Genomic_DNA.
DR   EMBL; AB001914; BAA21626.1; -; Genomic_DNA.
DR   EMBL; AB001914; BAA21627.1; -; Genomic_DNA.
DR   EMBL; D28513; BAA05871.1; -; mRNA.
DR   EMBL; D28514; BAA05872.1; -; mRNA.
DR   EMBL; D87995; BAA21793.1; -; mRNA.
DR   EMBL; D87993; BAA21791.1; -; mRNA.
DR   EMBL; D87994; BAA21792.1; -; mRNA.
DR   CCDS; CCDS73789.1; -. [P29122-2]
DR   CCDS; CCDS73790.1; -. [P29122-1]
DR   CCDS; CCDS73791.1; -. [P29122-5]
DR   CCDS; CCDS73793.1; -. [P29122-4]
DR   PIR; A39490; A39490.
DR   PIR; B39490; B39490.
DR   PIR; JC2191; JC2191.
DR   PIR; JC2192; JC2192.
DR   PIR; JC5570; JC5570.
DR   PIR; JC5571; JC5571.
DR   RefSeq; NP_001278238.1; NM_001291309.1.
DR   RefSeq; NP_002561.1; NM_002570.4. [P29122-1]
DR   RefSeq; NP_612192.1; NM_138319.3. [P29122-2]
DR   RefSeq; NP_612195.1; NM_138322.3. [P29122-3]
DR   RefSeq; NP_612196.1; NM_138323.2. [P29122-5]
DR   RefSeq; NP_612197.1; NM_138324.2. [P29122-4]
DR   RefSeq; NP_612198.2; NM_138325.3.
DR   AlphaFoldDB; P29122; -.
DR   SMR; P29122; -.
DR   BioGRID; 111083; 118.
DR   DIP; DIP-29903N; -.
DR   IntAct; P29122; 12.
DR   MINT; P29122; -.
DR   STRING; 9606.ENSP00000482760; -.
DR   BindingDB; P29122; -.
DR   ChEMBL; CHEMBL2951; -.
DR   GuidetoPHARMACOLOGY; 2386; -.
DR   MEROPS; S08.075; -.
DR   GlyCosmos; P29122; 4 sites, 1 glycan.
DR   GlyGen; P29122; 4 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P29122; -.
DR   PhosphoSitePlus; P29122; -.
DR   BioMuta; PCSK6; -.
DR   DMDM; 129542; -.
DR   EPD; P29122; -.
DR   MassIVE; P29122; -.
DR   MaxQB; P29122; -.
DR   PaxDb; 9606-ENSP00000482760; -.
DR   PeptideAtlas; P29122; -.
DR   ProteomicsDB; 54520; -. [P29122-1]
DR   ProteomicsDB; 54521; -. [P29122-2]
DR   ProteomicsDB; 54522; -. [P29122-3]
DR   ProteomicsDB; 54523; -. [P29122-4]
DR   ProteomicsDB; 54524; -. [P29122-5]
DR   ProteomicsDB; 54525; -. [P29122-6]
DR   ProteomicsDB; 54526; -. [P29122-7]
DR   ProteomicsDB; 54527; -. [P29122-8]
DR   Pumba; P29122; -.
DR   TopDownProteomics; P29122-3; -. [P29122-3]
DR   Antibodypedia; 1024; 331 antibodies from 33 providers.
DR   DNASU; 5046; -.
DR   Ensembl; ENST00000611716.5; ENSP00000482760.1; ENSG00000140479.18. [P29122-1]
DR   Ensembl; ENST00000611967.4; ENSP00000477768.1; ENSG00000140479.18. [P29122-4]
DR   Ensembl; ENST00000615296.4; ENSP00000478081.1; ENSG00000140479.18. [P29122-5]
DR   Ensembl; ENST00000618548.4; ENSP00000479496.1; ENSG00000140479.18. [P29122-2]
DR   GeneID; 5046; -.
DR   KEGG; hsa:5046; -.
DR   MANE-Select; ENST00000611716.5; ENSP00000482760.1; NM_002570.5; NP_002561.1.
DR   UCSC; uc032csi.2; human. [P29122-1]
DR   AGR; HGNC:8569; -.
DR   CTD; 5046; -.
DR   DisGeNET; 5046; -.
DR   GeneCards; PCSK6; -.
DR   HGNC; HGNC:8569; PCSK6.
DR   HPA; ENSG00000140479; Tissue enhanced (brain, liver, lymphoid tissue).
DR   MIM; 167405; gene.
DR   neXtProt; NX_P29122; -.
DR   OpenTargets; ENSG00000140479; -.
DR   PharmGKB; PA32895; -.
DR   VEuPathDB; HostDB:ENSG00000140479; -.
DR   eggNOG; KOG3525; Eukaryota.
DR   GeneTree; ENSGT00940000159506; -.
DR   HOGENOM; CLU_002976_4_1_1; -.
DR   InParanoid; P29122; -.
DR   OMA; CSTCTGQ; -.
DR   OrthoDB; 5474719at2759; -.
DR   PhylomeDB; P29122; -.
DR   TreeFam; TF314277; -.
DR   BRENDA; 3.4.21.61; 2681.
DR   BRENDA; 3.4.21.B25; 2681.
DR   PathwayCommons; P29122; -.
DR   Reactome; R-HSA-1181150; Signaling by NODAL.
DR   Reactome; R-HSA-167060; NGF processing.
DR   Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR   Reactome; R-HSA-8963889; Assembly of active LPL and LIPC lipase complexes.
DR   SignaLink; P29122; -.
DR   SIGNOR; P29122; -.
DR   BioGRID-ORCS; 5046; 10 hits in 329 CRISPR screens.
DR   ChiTaRS; PCSK6; human.
DR   GeneWiki; PCSK6; -.
DR   GenomeRNAi; 5046; -.
DR   Pharos; P29122; Tchem.
DR   PRO; PR:P29122; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; P29122; Protein.
DR   Bgee; ENSG00000140479; Expressed in C1 segment of cervical spinal cord and 180 other cell types or tissues.
DR   ExpressionAtlas; P29122; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:BHF-UCL.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0008201; F:heparin binding; IDA:BHF-UCL.
DR   GO; GO:0048406; F:nerve growth factor binding; IDA:BHF-UCL.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR   GO; GO:0009100; P:glycoprotein metabolic process; IDA:BHF-UCL.
DR   GO; GO:0032902; P:nerve growth factor production; IDA:BHF-UCL.
DR   GO; GO:0016486; P:peptide hormone processing; IDA:BHF-UCL.
DR   GO; GO:0034369; P:plasma lipoprotein particle remodeling; TAS:Reactome.
DR   GO; GO:0016485; P:protein processing; IDA:BHF-UCL.
DR   GO; GO:0030510; P:regulation of BMP signaling pathway; TAS:BHF-UCL.
DR   GO; GO:0032940; P:secretion by cell; IDA:BHF-UCL.
DR   GO; GO:0007354; P:zygotic determination of anterior/posterior axis, embryo; IEA:Ensembl.
DR   CDD; cd00064; FU; 4.
DR   CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.30.70.850; Peptidase S8, pro-domain; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR032778; GF_recep_IV.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR034182; Kexin/furin.
DR   InterPro; IPR002884; P_dom.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010909; PLAC.
DR   InterPro; IPR032815; S8_pro-domain.
DR   InterPro; IPR038466; S8_pro-domain_sf.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR   PANTHER; PTHR42884:SF8; PROPROTEIN CONVERTASE SUBTILISIN_KEXIN TYPE 6; 1.
DR   Pfam; PF14843; GF_recep_IV; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF16470; S8_pro-domain; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00261; FU; 5.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS50900; PLAC; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
DR   Genevisible; P29122; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cleavage on pair of basic residues;
KW   Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane; Protease;
KW   Reference proteome; Repeat; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..63
FT                   /evidence="ECO:0000255"
FT   PROPEP          64..149
FT                   /evidence="ECO:0000269|PubMed:9738469"
FT                   /id="PRO_0000027110"
FT   CHAIN           150..969
FT                   /note="Proprotein convertase subtilisin/kexin type 6"
FT                   /id="PRO_0000027111"
FT   DOMAIN          168..487
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DOMAIN          495..635
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT   REPEAT          692..739
FT                   /note="FU 1"
FT   REPEAT          743..790
FT                   /note="FU 2"
FT   REPEAT          794..838
FT                   /note="FU 3"
FT   REPEAT          842..887
FT                   /note="FU 4"
FT   REPEAT          895..943
FT                   /note="FU 5"
FT   DOMAIN          931..969
FT                   /note="PLAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          658..683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          695..930
FT                   /note="CRM (Cys-rich motif)"
FT   MOTIF           553..555
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..16
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        205
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        246
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        420
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   SITE            149..150
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000269|PubMed:9738469"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        914
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        932
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..167
FT                   /note="Missing (in isoform PACE4D)"
FT                   /evidence="ECO:0000303|PubMed:8179631"
FT                   /id="VSP_005427"
FT   VAR_SEQ         471
FT                   /note="K -> KGAAVAFWWTIGWPWNV (in isoform PACE4B)"
FT                   /evidence="ECO:0000303|PubMed:1741956"
FT                   /id="VSP_005428"
FT   VAR_SEQ         472..969
FT                   /note="Missing (in isoform PACE4B)"
FT                   /evidence="ECO:0000303|PubMed:1741956"
FT                   /id="VSP_005429"
FT   VAR_SEQ         621..664
FT                   /note="KLKEWSLILYGTAEHPYHTFSAHQSRSRMLELSAPELEPPKAAL -> DLET
FT                   PVANQLTTEERFVSTPSILFHWSVYLSWSQYHIVLITVAL (in isoform
FT                   PACE4D)"
FT                   /evidence="ECO:0000303|PubMed:8179631"
FT                   /id="VSP_005434"
FT   VAR_SEQ         621..652
FT                   /note="KLKEWSLILYGTAEHPYHTFSAHQSRSRMLEL -> DLETPVANQLTTEERE
FT                   PGLKHVFRWQIEQELW (in isoform PACE4C)"
FT                   /evidence="ECO:0000303|PubMed:8179631"
FT                   /id="VSP_005432"
FT   VAR_SEQ         621..623
FT                   /note="KLK -> NLD (in isoform PACE4CS)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005430"
FT   VAR_SEQ         624..969
FT                   /note="Missing (in isoform PACE4CS)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005431"
FT   VAR_SEQ         653..969
FT                   /note="Missing (in isoform PACE4C)"
FT                   /evidence="ECO:0000303|PubMed:8179631"
FT                   /id="VSP_005433"
FT   VAR_SEQ         665..969
FT                   /note="Missing (in isoform PACE4D)"
FT                   /evidence="ECO:0000303|PubMed:8179631"
FT                   /id="VSP_005435"
FT   VAR_SEQ         680..693
FT                   /note="AQSTPGSANILQTS -> G (in isoform PACE4A-II and
FT                   isoform PACE4E-II)"
FT                   /evidence="ECO:0000303|PubMed:9192737"
FT                   /id="VSP_005436"
FT   VAR_SEQ         901..969
FT                   /note="CDENCLSCAGSSRNCSRCKTGFTQLGTSCITNHTCSNADETFCEMVKSNRLC
FT                   ERKLFIQFCCRTCLLAG -> YGPPGGERQATVSSKGVPGGQSLSASSPGAGEGMLHHP
FT                   TVDRSPFTELLRGLRPFVHWMHICWVPAVGRHRAAAG (in isoform PACE4E-I
FT                   and isoform PACE4E-II)"
FT                   /evidence="ECO:0000303|PubMed:9192737"
FT                   /id="VSP_005437"
FT   VARIANT         502
FT                   /note="C -> R (in dbSNP:rs1058260)"
FT                   /id="VAR_051824"
FT   CONFLICT        639
FT                   /note="T -> I (in Ref. 6;
FT                   BAA21624/BAA21625/BAA21626/BAA21627)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   969 AA;  106420 MW;  A3599CC278D09B05 CRC64;
     MPPRAPPAPG PRPPPRAAAA TDTAAGAGGA GGAGGAGGPG FRPLAPRPWR WLLLLALPAA
     CSAPPPRPVY TNHWAVQVLG GPAEADRVAA AHGYLNLGQI GNLEDYYHFY HSKTFKRSTL
     SSRGPHTFLR MDPQVKWLQQ QEVKRRVKRQ VRSDPQALYF NDPIWSNMWY LHCGDKNSRC
     RSEMNVQAAW KRGYTGKNVV VTILDDGIER NHPDLAPNYD SYASYDVNGN DYDPSPRYDA
     SNENKHGTRC AGEVAASANN SYCIVGIAYN AKIGGIRMLD GDVTDVVEAK SLGIRPNYID
     IYSASWGPDD DGKTVDGPGR LAKQAFEYGI KKGRQGLGSI FVWASGNGGR EGDYCSCDGY
     TNSIYTISVS SATENGYKPW YLEECASTLA TTYSSGAFYE RKIVTTDLRQ RCTDGHTGTS
     VSAPMVAGII ALALEANSQL TWRDVQHLLV KTSRPAHLKA SDWKVNGAGH KVSHFYGFGL
     VDAEALVVEA KKWTAVPSQH MCVAASDKRP RSIPLVQVLR TTALTSACAE HSDQRVVYLE
     HVVVRTSISH PRRGDLQIYL VSPSGTKSQL LAKRLLDLSN EGFTNWEFMT VHCWGEKAEG
     QWTLEIQDLP SQVRNPEKQG KLKEWSLILY GTAEHPYHTF SAHQSRSRML ELSAPELEPP
     KAALSPSQVE VPEDEEDYTA QSTPGSANIL QTSVCHPECG DKGCDGPNAD QCLNCVHFSL
     GSVKTSRKCV SVCPLGYFGD TAARRCRRCH KGCETCSSRA ATQCLSCRRG FYHHQEMNTC
     VTLCPAGFYA DESQKNCLKC HPSCKKCVDE PEKCTVCKEG FSLARGSCIP DCEPGTYFDS
     ELIRCGECHH TCGTCVGPGR EECIHCAKNF HFHDWKCVPA CGEGFYPEEM PGLPHKVCRR
     CDENCLSCAG SSRNCSRCKT GFTQLGTSCI TNHTCSNADE TFCEMVKSNR LCERKLFIQF
     CCRTCLLAG
//