Reviewed, UniProtKB/Swiss-Prot Q5REC2 (NEC2_PONAB)

Names and origin

Protein names

Recommended name:
    Neuroendocrine convertase 2
      Short name=NEC 2
    EC=3.4.21.94
Alternative name(s):
    Prohormone convertase 2
    Proprotein convertase 2
      Short name=PC2

Gene names

Name:	PCSK2
Synonyms:	NEC2

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length	638 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues By similarity.
Catalytic activity	Release of protein hormones and neuropeptides from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds.
Subcellular location	Cytoplasmic vesicle › secretory vesicle By similarity. Note: Localized in the secretion granules By similarity.
Sequence similarities	Belongs to the peptidase S8 family. Furin subfamily.

Ontologies

Keywords
Cellular component	Cytoplasmic vesicle
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Gene Ontology (GO)
Cellular component	secretory granule Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Propeptide	26 – 109	84	Potential		PRO_0000262584
	Chain	110 – 638	529	Neuroendocrine convertase 2		PRO_0000262585
Regions
	Region	122 – 415	294	Catalytic
Sites
	Active site	167	1	Charge relay system By similarity
	Active site	208	1	Charge relay system By similarity
	Active site	384	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	375	1	N-linked (GlcNAc...) Potential
	Glycosylation	514	1	N-linked (GlcNAc...) Potential
	Glycosylation	524	1	N-linked (GlcNAc...) Potential
	Disulfide bond	225 ↔ 376		By similarity
	Disulfide bond	317 ↔ 347		By similarity
	Disulfide bond	468 ↔ 494		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5REC2-1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 789B0D2EFD32F396	FASTA	638	70,566
	10 20 30 40 50 60 MKGGCVSQWK AAAGFLFCVM VFASAERPVF TNHFLVELHK GGEDEARQVA AEHGFGVRKL 70 80 90 100 110 120 PFAEGLYHFY HNGLAKAKRR RSLHHKQQLE RDPRVKMALQ QEGFDRKKRG YRDINEIDIN 130 140 150 160 170 180 MNDPLFTKQW YLINTGQADG TPGLDLNVAE AWELGYTGKG VTIGIMDDGI DYLHPDLASN 190 200 210 220 230 240 YNAEASYDFS SNDPYPYPRY TDDWFNSHGT RCAGEVSAAA NNNICGVGVA YNSKVAGIRM 250 260 270 280 290 300 LDQPFMTDII EASSISHMPQ LIDIYSASWG PTDNGKTVDG PRELTLQAMA DGVNKGRGGK 310 320 330 340 350 360 GSIYVWASGD GGSYDDCNCD GYASSMWTIS INSAINDGRT ALYDESCSST LASTFSNGRK 370 380 390 400 410 420 RNPEAGVATT DLYGNCTLRH SGTSAAAPEA AGVFALALEA NLGLTWRDMQ HLTVLTSKRN 430 440 450 460 470 480 QLHDEVHQWR RNGVGLEFNH LFGYGVLDAG AMVKMAKDWK TVPERFHCVG GSVQDPEKIP 490 500 510 520 530 540 STGKLVLTLT TDACEGKENF VRYLEHVQAV ITVNATRRGD LNINMTSPMG TKSILLSRRP 550 560 570 580 590 600 RDDDSKVGFD KWPFMTTHTW GEDARGTWTL ELGFVGSAPQ KGVLKEWTLM LHGTQSAPYI 610 620 630 DQVVRDYQSK LAMSKKEELE EELDEAVERS LKSILNKN

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR857610 mRNA. Translation: CAH89885.1.
RefSeq	NP_001124879.1.
UniGene	Pab.18041
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	100171744.
Organism-specific databases
CTD	100171744.
Phylogenomic databases
HOVERGEN	Q5REC2.
OMA	NYNADAS.
Enzyme and pathway databases
BRENDA	3.4.21.94. 269192.
Family and domain databases
InterPro	IPR000209. Peptidase_S8/S53. IPR015500. Peptidase_S8_subtilisin-rel. IPR002884. PrprotnconvertsP. [Graphical view]
Gene3D	G3DSA:3.40.50.200. Pept_S8_S53. 1 hit.
PANTHER	PTHR10795. SubtilSerProt. 1 hit.
Pfam	PF01483. P_proprotein. 1 hit. PF00082. Peptidase_S8. 1 hit. [Graphical view]
PRINTS	PR00723. SUBTILISIN.
ProDom	PD000717. PrprotnconvertsP. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00136. SUBTILASE_ASP. 1 hit. PS00137. SUBTILASE_HIS. 1 hit. PS00138. SUBTILASE_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NEC2_PONAB

Accession

Primary (citable) accession number: Q5REC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	December 21, 2004
Last modified:	November 3, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)