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Proprotein convertase subtilisin/kexin type 5 (EC 3.4.21.-) (Proprotein convertase 5) (PC5) (Proprotein convertase 6) (PC6) (hPC6) (Subtilisin/kexin-like protease PC5)

 PCSK5_HUMAN             Reviewed;        1860 AA.
Q92824; F5H2G7; Q13527; Q96EP4;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
16-NOV-2011, sequence version 4.
22-NOV-2017, entry version 178.
RecName: Full=Proprotein convertase subtilisin/kexin type 5;
EC=3.4.21.-;
AltName: Full=Proprotein convertase 5;
Short=PC5;
AltName: Full=Proprotein convertase 6;
Short=PC6;
Short=hPC6;
AltName: Full=Subtilisin/kexin-like protease PC5;
Flags: Precursor;
Name=PCSK5; Synonyms=PC5, PC6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PC6A), AND ALTERNATIVE SPLICING.
TISSUE=T-cell;
PubMed=8755538; DOI=10.1073/pnas.93.15.7695;
Miranda L., Wolf J., Pichuantes S., Duke R., Franzusoff A.;
"Isolation of the human PC6 gene encoding the putative host protease
for HIV-1 gp160 processing in CD4+ T lymphocytes.";
Proc. Natl. Acad. Sci. U.S.A. 93:7695-7700(1996).
[2]
SEQUENCE REVISION.
Franzusoff A., Miranda L., Wolf J., Pichuantes S., Lu Y., Duke R.;
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PC6A).
TISSUE=Lymph node;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PC6A).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 15-913 (ISOFORM PC6A).
Reudelhuber T.L.;
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1166-1860 (ISOFORM PC6B).
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
FUNCTION IN PREGNANCY ESTABLISHMENT.
PubMed=19764806; DOI=10.1021/pr900381a;
Kilpatrick L.M., Stephens A.N., Hardman B.M., Salamonsen L.A., Li Y.,
Stanton P.G., Nie G.;
"Proteomic identification of caldesmon as a physiological substrate of
proprotein convertase 6 in human uterine decidual cells essential for
pregnancy establishment.";
J. Proteome Res. 8:4983-4992(2009).
[10]
FUNCTION IN PREGNANCY ESTABLISHMENT.
PubMed=20555025; DOI=10.1210/en.2010-0326;
Heng S., Paule S., Hardman B., Li Y., Singh H., Rainczuk A.,
Stephens A.N., Nie G.;
"Posttranslational activation of bone morphogenetic protein 2 is
mediated by proprotein convertase 6 during decidualization for
pregnancy establishment.";
Endocrinology 151:3909-3917(2010).
[11]
FUNCTION.
PubMed=22740495; DOI=10.1093/humrep/des203;
Paule S., Aljofan M., Simon C., Rombauts L.J., Nie G.;
"Cleavage of endometrial alpha-integrins into their functional forms
is mediated by proprotein convertase 5/6.";
Hum. Reprod. 27:2766-2774(2012).
-!- FUNCTION: Serine endoprotease that processes various proproteins
by cleavage at paired basic amino acids, recognizing the RXXX[KR]R
consensus motif. Likely functions in the constitutive and
regulated secretory pathways. Plays an essential role in pregnancy
establishment by proteolytic activation of a number of important
factors such as BMP2, CALD1 and alpha-integrins.
{ECO:0000269|PubMed:19764806, ECO:0000269|PubMed:20555025,
ECO:0000269|PubMed:22740495}.
-!- INTERACTION:
Q6UY14-3:ADAMTSL4; NbExp=4; IntAct=EBI-11956269, EBI-10173507;
Q02930-3:CREB5; NbExp=4; IntAct=EBI-11956269, EBI-10192698;
O76003:GLRX3; NbExp=3; IntAct=EBI-751290, EBI-374781;
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-751290, EBI-10172290;
P60410:KRTAP10-8; NbExp=4; IntAct=EBI-11956269, EBI-10171774;
Q9BQ66:KRTAP4-12; NbExp=3; IntAct=EBI-751290, EBI-739863;
P26371:KRTAP5-9; NbExp=3; IntAct=EBI-751290, EBI-3958099;
Q5T752:LCE1D; NbExp=4; IntAct=EBI-11956269, EBI-11741311;
Q5TA81:LCE2C; NbExp=4; IntAct=EBI-11956269, EBI-11973993;
Q5T5A8:LCE3C; NbExp=3; IntAct=EBI-751290, EBI-10245291;
Q99750:MDFI; NbExp=4; IntAct=EBI-11956269, EBI-724076;
P50222:MEOX2; NbExp=3; IntAct=EBI-751290, EBI-748397;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-751290, EBI-945833;
Q7Z417:NUFIP2; NbExp=3; IntAct=EBI-751290, EBI-1210753;
O75716:STK16; NbExp=3; IntAct=EBI-751290, EBI-749295;
Q8WW24:TEKT4; NbExp=4; IntAct=EBI-11956269, EBI-750487;
Q96EG3:ZNF837; NbExp=4; IntAct=EBI-11956269, EBI-11962574;
-!- SUBCELLULAR LOCATION: Isoform PC6A: Secreted. Note=Secreted
through the regulated secretory pathway. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform PC6B: Endomembrane system; Single-
pass type I membrane protein. Note=Type I membrane protein
localized to a paranuclear post-Golgi network compartment in
communication with early endosomes. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=PC6B; Synonyms=Long;
IsoId=Q92824-1; Sequence=Displayed;
Name=PC6A; Synonyms=Short;
IsoId=Q92824-2; Sequence=VSP_042017, VSP_042018;
-!- TISSUE SPECIFICITY: Expressed in T-lymphocytes.
-!- DOMAIN: The propeptide domain acts as an intramolecular chaperone
assisting the folding of the zymogen within the endoplasmic
reticulum.
-!- DOMAIN: AC 1 and AC 2 (clusters of acidic amino acids) contain
sorting information. AC 1 directs TGN localization and interacts
with the TGN sorting protein PACS-1 (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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EMBL; U56387; AAC50643.2; -; mRNA.
EMBL; AL834522; CAD39178.1; -; mRNA.
EMBL; AL359253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL353607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL391868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL589653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471089; EAW62575.1; -; Genomic_DNA.
EMBL; BC012064; AAH12064.1; -; mRNA.
EMBL; U49114; AAA91807.1; -; mRNA.
EMBL; AK122718; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS55320.1; -. [Q92824-1]
CCDS; CCDS6652.1; -. [Q92824-2]
PIR; G02428; G02428.
PIR; JC6148; JC6148.
RefSeq; NP_001177411.1; NM_001190482.1. [Q92824-1]
RefSeq; NP_006191.2; NM_006200.5. [Q92824-2]
UniGene; Hs.368542; -.
UniGene; Hs.732073; -.
ProteinModelPortal; Q92824; -.
SMR; Q92824; -.
BioGrid; 111152; 32.
IntAct; Q92824; 53.
MINT; MINT-1474189; -.
STRING; 9606.ENSP00000446280; -.
BindingDB; Q92824; -.
ChEMBL; CHEMBL2826; -.
GuidetoPHARMACOLOGY; 2385; -.
MEROPS; S08.076; -.
iPTMnet; Q92824; -.
PhosphoSitePlus; Q92824; -.
BioMuta; PCSK5; -.
DMDM; 357529585; -.
PaxDb; Q92824; -.
PeptideAtlas; Q92824; -.
PRIDE; Q92824; -.
DNASU; 5125; -.
Ensembl; ENST00000376752; ENSP00000365943; ENSG00000099139. [Q92824-2]
Ensembl; ENST00000545128; ENSP00000446280; ENSG00000099139. [Q92824-1]
GeneID; 5125; -.
KEGG; hsa:5125; -.
UCSC; uc004ajz.5; human. [Q92824-1]
CTD; 5125; -.
DisGeNET; 5125; -.
EuPathDB; HostDB:ENSG00000099139.13; -.
GeneCards; PCSK5; -.
HGNC; HGNC:8747; PCSK5.
HPA; HPA031072; -.
MIM; 600488; gene.
neXtProt; NX_Q92824; -.
OpenTargets; ENSG00000099139; -.
PharmGKB; PA33093; -.
eggNOG; KOG3525; Eukaryota.
eggNOG; COG1404; LUCA.
eggNOG; COG4935; LUCA.
GeneTree; ENSGT00750000117358; -.
HOGENOM; HOG000192536; -.
HOVERGEN; HBG008705; -.
InParanoid; Q92824; -.
KO; K08654; -.
OMA; SSCRTCE; -.
OrthoDB; EOG091G05HI; -.
PhylomeDB; Q92824; -.
TreeFam; TF314277; -.
BRENDA; 3.4.21.B26; 2681.
Reactome; R-HSA-167060; NGF processing.
Reactome; R-HSA-8963889; Assembly of active LPL and LIPC lipase complexes.
SignaLink; Q92824; -.
ChiTaRS; PCSK5; human.
GeneWiki; PCSK5; -.
GenomeRNAi; 5125; -.
PMAP-CutDB; Q92824; -.
PRO; PR:Q92824; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000099139; -.
CleanEx; HS_PCSK5; -.
ExpressionAtlas; Q92824; baseline and differential.
Genevisible; Q92824; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; ISS:BHF-UCL.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030141; C:secretory granule; ISS:BHF-UCL.
GO; GO:0004175; F:endopeptidase activity; EXP:Reactome.
GO; GO:0008233; F:peptidase activity; IDA:MGI.
GO; GO:0042277; F:peptide binding; ISS:BHF-UCL.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:BHF-UCL.
GO; GO:0003279; P:cardiac septum development; IEA:Ensembl.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
GO; GO:0042089; P:cytokine biosynthetic process; ISS:BHF-UCL.
GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
GO; GO:0007566; P:embryo implantation; ISS:BHF-UCL.
GO; GO:0048566; P:embryonic digestive tract development; IMP:BHF-UCL.
GO; GO:0048706; P:embryonic skeletal system development; IMP:BHF-UCL.
GO; GO:0007507; P:heart development; ISS:BHF-UCL.
GO; GO:0001822; P:kidney development; IMP:BHF-UCL.
GO; GO:0035108; P:limb morphogenesis; ISS:BHF-UCL.
GO; GO:0032455; P:nerve growth factor processing; TAS:Reactome.
GO; GO:0043043; P:peptide biosynthetic process; IDA:BHF-UCL.
GO; GO:0016486; P:peptide hormone processing; IDA:BHF-UCL.
GO; GO:0016485; P:protein processing; IDA:BHF-UCL.
GO; GO:0051004; P:regulation of lipoprotein lipase activity; TAS:Reactome.
GO; GO:0002001; P:renin secretion into blood stream; IEP:BHF-UCL.
GO; GO:0030323; P:respiratory tube development; ISS:BHF-UCL.
GO; GO:0006465; P:signal peptide processing; IDA:HGNC.
GO; GO:0019058; P:viral life cycle; IEP:BHF-UCL.
CDD; cd04059; Peptidases_S8_Protein_converta; 1.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 3.40.50.200; -; 1.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR006212; Furin_repeat.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR032778; GF_recep_IV.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR034182; Kexin/furin.
InterPro; IPR009020; Peptidase/Inhibitor_I9.
InterPro; IPR000209; Peptidase_S8/S53_dom.
InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
InterPro; IPR023827; Peptidase_S8_Asp-AS.
InterPro; IPR022398; Peptidase_S8_His-AS.
InterPro; IPR023828; Peptidase_S8_Ser-AS.
InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
InterPro; IPR002884; PrprotnconvertsP.
InterPro; IPR032815; S8_pro-domain.
InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
Pfam; PF14843; GF_recep_IV; 1.
Pfam; PF01483; P_proprotein; 1.
Pfam; PF00082; Peptidase_S8; 1.
Pfam; PF16470; S8_pro-domain; 1.
PRINTS; PR00723; SUBTILISIN.
SMART; SM00181; EGF; 16.
SMART; SM01411; Ephrin_rec_like; 8.
SMART; SM00261; FU; 22.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF52743; SSF52743; 1.
SUPFAM; SSF54897; SSF54897; 1.
SUPFAM; SSF57184; SSF57184; 7.
PROSITE; PS51829; P_HOMO_B; 1.
PROSITE; PS00136; SUBTILASE_ASP; 1.
PROSITE; PS00137; SUBTILASE_HIS; 1.
PROSITE; PS00138; SUBTILASE_SER; 1.
1: Evidence at protein level;
Alternative splicing; Cleavage on pair of basic residues;
Complete proteome; Glycoprotein; Hydrolase; Membrane; Pregnancy;
Protease; Reference proteome; Repeat; Secreted; Serine protease;
Signal; Transmembrane; Transmembrane helix; Zymogen.
SIGNAL 1 32 {ECO:0000250}.
PROPEP 33 114 {ECO:0000250}.
/FTId=PRO_0000027102.
CHAIN 115 1860 Proprotein convertase subtilisin/kexin
type 5.
/FTId=PRO_0000027103.
TOPO_DOM 115 1743 Extracellular. {ECO:0000255}.
TRANSMEM 1744 1764 Helical. {ECO:0000255}.
TOPO_DOM 1765 1860 Cytoplasmic. {ECO:0000255}.
DOMAIN 166 453 Peptidase S8.
DOMAIN 461 601 P/Homo B. {ECO:0000255|PROSITE-
ProRule:PRU01173}.
REPEAT 630 680 FU 1.
REPEAT 683 730 FU 2.
REPEAT 734 777 FU 3.
REPEAT 779 824 FU 4.
REPEAT 832 879 FU 5.
DOMAIN 869 913 PLAC.
REPEAT 882 927 FU 6.
REPEAT 929 979 FU 7.
REPEAT 982 1028 FU 8.
REPEAT 1032 1077 FU 9.
REPEAT 1079 1121 FU 10.
REPEAT 1125 1168 FU 11.
REPEAT 1177 1221 FU 12.
REPEAT 1225 1272 FU 13.
REPEAT 1274 1318 FU 14.
REPEAT 1320 1363 FU 15.
REPEAT 1365 1411 FU 16.
REPEAT 1415 1461 FU 17.
REPEAT 1465 1510 FU 18.
REPEAT 1514 1559 FU 19.
REPEAT 1563 1610 FU 20.
REPEAT 1614 1659 FU 21.
REPEAT 1665 1712 FU 22.
REGION 636 1727 CRM (Cys-rich motif).
REGION 1807 1826 AC 1. {ECO:0000250}.
REGION 1838 1860 AC 2. {ECO:0000250}.
MOTIF 519 521 Cell attachment site. {ECO:0000255}.
COMPBIAS 1812 1853 Asp-rich.
ACT_SITE 171 171 Charge relay system. {ECO:0000250}.
ACT_SITE 212 212 Charge relay system. {ECO:0000250}.
ACT_SITE 386 386 Charge relay system. {ECO:0000250}.
SITE 114 115 Cleavage; by autolysis. {ECO:0000250}.
CARBOHYD 225 225 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 381 381 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 665 665 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 752 752 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 802 802 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 852 852 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1014 1014 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1191 1191 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1290 1290 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1497 1497 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1685 1685 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1707 1707 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 876 913 GEYVDEHGHCQTCEASCAKCQGPTQEDCTTCPMTRIFD ->
ATEESWAEGGFCMLVKKNNLCQRKVLQQLCCKTCTFQG
(in isoform PC6A).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:8755538,
ECO:0000303|Ref.7}.
/FTId=VSP_042017.
VAR_SEQ 914 1860 Missing (in isoform PC6A).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:8755538,
ECO:0000303|Ref.7}.
/FTId=VSP_042018.
CONFLICT 2 2 G -> D (in Ref. 1; AAC50643).
{ECO:0000305}.
CONFLICT 4 4 G -> E (in Ref. 1; AAC50643).
{ECO:0000305}.
CONFLICT 118 118 F -> S (in Ref. 1; AAC50643).
{ECO:0000305}.
CONFLICT 121 121 A -> V (in Ref. 1; AAC50643).
{ECO:0000305}.
CONFLICT 511 511 R -> A (in Ref. 7; AAA91807).
{ECO:0000305}.
CONFLICT 601 601 Q -> R (in Ref. 1; AAC50643).
{ECO:0000305}.
SEQUENCE 1860 AA; 206942 MW; 96B3E7C8215BCC85 CRC64;
MGWGSRCCCP GRLDLLCVLA LLGGCLLPVC RTRVYTNHWA VKIAGGFPEA NRIASKYGFI
NIGQIGALKD YYHFYHSRTI KRSVISSRGT HSFISMEPKV EWIQQQVVKK RTKRDYDFSR
AQSTYFNDPK WPSMWYMHCS DNTHPCQSDM NIEGAWKRGY TGKNIVVTIL DDGIERTHPD
LMQNYDALAS CDVNGNDLDP MPRYDASNEN KHGTRCAGEV AAAANNSHCT VGIAFNAKIG
GVRMLDGDVT DMVEAKSVSF NPQHVHIYSA SWGPDDDGKT VDGPAPLTRQ AFENGVRMGR
RGLGSVFVWA SGNGGRSKDH CSCDGYTNSI YTISISSTAE SGKKPWYLEE CSSTLATTYS
SGESYDKKII TTDLRQRCTD NHTGTSASAP MAAGIIALAL EANPFLTWRD VQHVIVRTSR
AGHLNANDWK TNAAGFKVSH LYGFGLMDAE AMVMEAEKWT TVPRQHVCVE STDRQIKTIR
PNSAVRSIYK ASGCSDNPNR HVNYLEHVVV RITITHPRRG DLAIYLTSPS GTRSQLLANR
LFDHSMEGFK NWEFMTIHCW GERAAGDWVL EVYDTPSQLR NFKTPGKLKE WSLVLYGTSV
QPYSPTNEFP KVERFRYSRV EDPTDDYGTE DYAGPCDPEC SEVGCDGPGP DHCNDCLHYY
YKLKNNTRIC VSSCPPGHYH ADKKRCRKCA PNCESCFGSH GDQCMSCKYG YFLNEETNSC
VTHCPDGSYQ DTKKNLCRKC SENCKTCTEF HNCTECRDGL SLQGSRCSVS CEDGRYFNGQ
DCQPCHRFCA TCAGAGADGC INCTEGYFME DGRCVQSCSI SYYFDHSSEN GYKSCKKCDI
SCLTCNGPGF KNCTSCPSGY LLDLGMCQMG AICKDGEYVD EHGHCQTCEA SCAKCQGPTQ
EDCTTCPMTR IFDDGRCVSN CPSWKFEFEN QCHPCHHTCQ RCQGSGPTHC TSCGADNYGR
EHFLYQGECG DSCPEGHYAT EGNTCLPCPD NCELCHSVHV CTRCMKGYFI APTNHTCQKL
ECGQGEVQDP DYEECVPCEE GCLGCSLDDP GTCTSCAMGY YRFDHHCYKT CPEKTYSEEV
ECKACDSNCG SCDQNGCYWC EEGFFLLGGS CVRKCGPGFY GDQEMGECES CHRACETCTG
PGHDECSSCQ EGLQLLRGMC VHATKTQEEG KFWNDILRKL QPCHSSCKTC NGSATLCTSC
PKGAYLLAQA CVSSCPQGTW PSVRSGSCEN CTEACAICSG ADLCKKCQMQ PGHPLFLHEG
RCYSKCPEGS YAEDGICERC SSPCRTCEGN ATNCHSCEGG HVLHHGVCQE NCPERHVAVK
GVCKHCPEMC QDCIHEKTCK ECTPEFFLHD DMCHQSCPRG FYADSRHCVP CHKDCLECSG
PKADDCELCL ESSWVLYDGL CLEECPAGTY YEKETKECRD CHKSCLTCSS SGTCTTCQKG
LIMNPRGSCM ANEKCSPSEY WDEDAPGCKP CHVKCFHCMG PAEDQCQTCP MNSLLLNTTC
VKDCPEGYYA DEDSNRCAHC HSSCRTCEGR HSRQCHSCRP GWFQLGKECL LQCREGYYAD
NSTGRCERCN RSCKGCQGPR PTDCLSCDRF FFLLRSKGEC HRSCPDHYYV EQSTQTCERC
HPTCDQCKGK GALNCLSCVW SYHLMGGICT SDCLVGEYRV GEGEKFNCEK CHESCMECKG
PGAKNCTLCP ANLVLHMDDS HCLHCCNTSD PPSAQECCDC QDTTDECILR TSKVRPATEH
FKTALFITSS MMLVLLLGAA VVVWKKSRGR VQPAAKAGYE KLADPNKSYS SYKSSYREST
SFEEDQVIEY RDRDYDEDDD DDIVYMGQDG TVYRKFKYGL LDDDDIDELE YDDESYSYYQ


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