PCSK5_BRACL
ID PCSK5_BRACL Reviewed; 1696 AA.
AC Q9NJ15; Q9NJ14; Q9NJ16;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Proprotein convertase subtilisin/kexin type 5;
DE EC=3.4.21.-;
DE AltName: Full=Proprotein convertase PC6-like;
DE Short=aPC6;
DE Flags: Precursor;
GN Name=PC6;
OS Branchiostoma californiense (California lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomidae; Branchiostoma.
OX NCBI_TaxID=7738;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
RX PubMed=10708868; DOI=10.1016/s0167-4838(99)00283-6;
RA Oliva A.A. Jr., Chan S.J., Steiner D.F.;
RT "Evolution of the prohormone convertases: identification of a homologue of
RT PC6 in the protochordate amphioxus.";
RL Biochim. Biophys. Acta 1477:338-348(2000).
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 and regulated
CC secretory pathways. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform A]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform C]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform B]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=B;
CC IsoId=Q9NJ15-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q9NJ15-2; Sequence=VSP_005444, VSP_005445;
CC Name=C;
CC IsoId=Q9NJ15-3; Sequence=VSP_005442, VSP_005443;
CC -!- DOMAIN: The propeptide domain acts as an intramolecular chaperone
CC assisting the folding of the zymogen within the endoplasmic reticulum.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AF184615; AAF26300.1; -; mRNA.
DR EMBL; AF184616; AAF26301.1; -; mRNA.
DR EMBL; AF184617; AAF26302.1; -; mRNA.
DR AlphaFoldDB; Q9NJ15; -.
DR SMR; Q9NJ15; -.
DR PRIDE; Q9NJ15; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00064; FU; 12.
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; 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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR043601; Rspo_Fu-CRD_dom.
DR InterPro; IPR032815; S8_pro-domain.
DR InterPro; IPR038466; S8_pro-domain_sf.
DR Pfam; PF15913; Furin-like_2; 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; 9.
DR SMART; SM00261; FU; 18.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52743; SSF52743; 1.
DR SUPFAM; SSF57184; SSF57184; 8.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Cleavage on pair of basic residues;
KW Glycoprotein; Hydrolase; Membrane; Protease; Repeat; Secreted;
KW Serine protease; Signal; Transmembrane; Transmembrane helix; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..110
FT /evidence="ECO:0000255"
FT /id="PRO_0000027108"
FT CHAIN 111..1696
FT /note="Proprotein convertase subtilisin/kexin type 5"
FT /id="PRO_0000027109"
FT TOPO_DOM 111..1618
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1619..1639
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1640..1696
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 167..487
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 495..638
FT /note="P/Homo B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT REGION 111..488
FT /note="Catalytic"
FT REGION 643..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..1649
FT /note="CRM (Cys-rich motif)"
FT COMPBIAS 643..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 192
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 233
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 407
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT SITE 110..111
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 885
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1259..1323
FT /note="DDTILDRGECITSCGPGEYMDRREKKCKACHPTCKECSDEYDDTCTACNDGF
FT LLTDASSCEAGCP -> AENQNQASFCPFAPREVSVLAELALGHLRYSLTDVPPQSNSP
FT PDTVLGADRARLTTATSAAGRCA (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10708868"
FT /id="VSP_005442"
FT VAR_SEQ 1288..1343
FT /note="CHPTCKECSDEYDDTCTACNDGFLLTDASSCEAGCPPGQFLHHGDCDSCHRE
FT CKTC -> IARCVDRRDRSWCDLVLRFNFCVRRYFVKRCCGTCKLYMEDRPMRRGSSQP
FT TQGRN (in isoform A)"
FT /evidence="ECO:0000303|PubMed:10708868"
FT /id="VSP_005444"
FT VAR_SEQ 1324..1696
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10708868"
FT /id="VSP_005443"
FT VAR_SEQ 1344..1696
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:10708868"
FT /id="VSP_005445"
SQ SEQUENCE 1696 AA; 188411 MW; 281CBE1784257CBD CRC64;
MPPAIVILAL FTAALCAVNL RTVAADGPRI YRNEWALHVE GGTAAADRLA SKHGFINKGQ
IGSLEDHYLF VHRRTWKRSL RSSSHRHALL QREPEVRWLQ QQVVKRRVKR RVKRVYSMYP
WEQRVQHSSP QVNNPAQQDN LWDPHFNDEK WDKMWYLHCD RPEFACQWSD MNVEAAWKKG
YTGKGVVVSI LDDGSETDHP DLAGNYDPDA SSDINGGTLD PTPRYEYTNE NRHGTRCAGE
VAAMGNNSFC SVGVAYKASI GGVRMLDGDV TDSVEAASLG LNPQHIMIYS ASWGPDDDGK
TVDGPANLAQ KTFQAGAENG RDKLGSIFVW ASGNGGRTHD SCGCDGYTNS IYTISVSSAS
EQGKVPWYLE PCASTLATTY SSGAPHERKV ITTDLRKGCT ESHTGTSASA PMAAGILALA
LEANPMLTWR DMQYIVVMAA NPSPLDRDTE SAYPRDPRKE SDFVTNGAGL RVSHNFGFGL
MDAGKMVELA ESWRRVPEQH VCEEDPNAQQ RAITKGETIV DTKTTGGCNG TDHHVKYLEH
VVVEISLDHP CRGHLSIHIT SPSGTRSTLL PERQFDSSSD GLKDWAFMTT HCWGEQPEGD
WILEVKDLGQ QNCQRYGLRT VLPVLRKWKL ILYGTAEHPL YKRDEESRPH TPQTREEPTD
EEECEDGDYY DRSKQRCRHC HDSCATCHGR HSGQCLSCHE GNYFVEDEGT CSEECGQGYY
KDEEERKCLD CSADCLTCQV SADHCTSCDD EDGLKLFENT CVAQCSEGRY MDENDVCQDC
DDSCDTCTGP DATDCVTCAD EDLLQESQCV ESCSSGYFQQ EYECLKCHAT CASCSGSRDD
QCLTCSGHLE LDEDTHRCIT SCEDGEYGTE EGKCEDCNII CKKCNGSQAD QCLECHHDTN
LYDTTCVQYC GNRRYPENGE CHPCHPSCLG CIGGEINQCN QCITDYEGED HFLYQGTCHV
TCPPGLYGDT TDQVCKACAP GCIACDGPAD NQCTLCEEER APTDGRCQSE GSQTDEAECA
EGCHSCEEGP DICDSCDEDY YLTEDTCVRR TNCPSFTYPD DQDRECRPCH DNCEACDGPN
NQNCNSCKEG FYKTPDGCST GCPNRYYKDD TNKECKPCDS SCFTCSGPAS FHCLSCADGD
FLHESSCRST CPAGFIGNAE SHECVESSCE QDQYYSSETG RCEDCPYNCR ACDNDGDCAE
CAPTYIVVDG RCRPEETCED GEYQDRDRDT AELSCRPCHQ SCKTCSGPSD TDCDSCKGDD
TILDRGECIT SCGPGEYMDR REKKCKACHP TCKECSDEYD DTCTACNDGF LLTDASSCEA
GCPPGQFLHH GDCDSCHREC KTCDGPHHDN CLSCQPGSYL NDQQCSTHCP EGTFEETYED
DSGETVLQCR LCHVNCKTCH GEGEEDCMEC ANDIKYKQDG RCVTECQEGH YPDLTNECQQ
CWSDCETCDG PRNDQCVTCP YNYYLVLGKC LEDCPEGYYD TMRQEKECGE CHPSCATCNE
GGNYNCLSCP YGSKLGEGVC YPMCEEHEYY VEKTQICEEC DNSCKTCRGS TAHDCLSCEA
PYGYHAMKHL CTACCEEGSP ENEYCCICHE STRLCITDRE AEGVQFSSAD SIPTNVAYIA
VATFICVVIV VLFFVVFGML QARSNGRLCW AHKYQQVPTT RYEKMNDHVN ILSQEDFYNE
DSLSEDEIHS IDSTRH
