PCSK6_HUMAN
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 03-AUG-2022, entry version 210.
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}.
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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; 112.
DR DIP; DIP-29903N; -.
DR IntAct; P29122; 11.
DR MINT; P29122; -.
DR STRING; 9606.ENSP00000482760; -.
DR BindingDB; P29122; -.
DR ChEMBL; CHEMBL2951; -.
DR GuidetoPHARMACOLOGY; 2386; -.
DR MEROPS; S08.075; -.
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; P29122; -.
DR PeptideAtlas; P29122; -.
DR PRIDE; 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 TopDownProteomics; P29122-3; -. [P29122-3]
DR Antibodypedia; 1024; 320 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 CTD; 5046; -.
DR DisGeNET; 5046; -.
DR GeneCards; PCSK6; -.
DR HGNC; HGNC:8569; PCSK6.
DR HPA; ENSG00000140479; Group enriched (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; 308083at2759; -.
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 272 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 179 other tissues.
DR ExpressionAtlas; P29122; baseline and differential.
DR Genevisible; P29122; HS.
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:0016485; P:protein processing; IDA:BHF-UCL.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; TAS:BHF-UCL.
DR GO; GO:0051004; P:regulation of lipoprotein lipase activity; TAS:Reactome.
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; 3.30.70.850; -; 1.
DR Gene3D; 3.40.50.200; -; 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 Pfam; PF14843; GF_recep_IV; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF08686; PLAC; 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; SSF49785; 1.
DR SUPFAM; SSF52743; SSF52743; 1.
DR SUPFAM; SSF57184; SSF57184; 2.
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.
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; BAA21624/BAA21625/BAA21626/
FT 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
