Q9NXS2 (QPCTL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutaminyl-peptide cyclotransferase-like protein
EC=2.3.2.5

Alternative name(s):
Golgi-resident glutaminyl-peptide cyclotransferase
isoQC
Short name=gQC

Gene names

Name:

QPCTL

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Responsible for the biosynthesis of pyroglutamyl peptides. Ref.5 Ref.7
Catalytic activity	L-glutaminyl-peptide = 5-oxoprolyl-peptide + NH3. Ref.5 Ref.7
Cofactor	Binds 1 zinc ion per subunit. Ref.7
Subcellular location	Golgi apparatus membrane; Single-pass type I membrane protein Ref.5.
Sequence similarities	Belongs to the glutaminyl-peptide cyclotransferase family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase Inferred from direct assay Ref.7. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	glutaminyl-peptide cyclotransferase activity Inferred from direct assay Ref.7. Source: UniProtKB peptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
POLR1E	Q9GZS1	1	EBI-1052839,EBI-359458

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 382

382

Glutaminyl-peptide cyclotransferase-like protein

PRO_0000302002

Regions

Transmembrane

35 – 55

21

Helical; Potential

Sites

Active site

225

1

Proton acceptor

Active site

269

1

Proton acceptor

Metal binding

186

1

Zinc; catalytic

Metal binding

226

1

Zinc; catalytic

Metal binding

351

1

Zinc; catalytic

Natural variations

Natural variant

214

1

P → L.
Corresponds to variant rs28708996 [ dbSNP | Ensembl ].

VAR_034937

Experimental info

Sequence conflict

118 – 211

94

Missing in AAH11553. Ref.4

Sequence conflict

295

1

I → T in BAD96356. Ref.2

Sequence conflict

321

1

F → S in BAA90938. Ref.1

Sequence conflict

321

1

F → S in BAD18747. Ref.1

Sequence conflict

334

1

R → G in BAD96356. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

382

Helix Strand Turn

Details...

Helix

78 – 84

7

Helix

90 – 96

7

Helix

99 – 101

3

Helix

113 – 125

13

Beta strand

131 – 139

9

Beta strand

146 – 148

3

Beta strand

150 – 155

6

Beta strand

159 – 168

10

Turn

185 – 187

3

Helix

188 – 200

13

Helix

202 – 210

9

Beta strand

214 – 222

9

Helix

241 – 249

9

Turn

258 – 261

4

Beta strand

262 – 269

8

Helix

283 – 285

3

Helix

286 – 301

16

Beta strand

313 – 315

3

Helix

329 – 332

4

Beta strand

338 – 342

5

Turn

348 – 351

4

Helix

357 – 359

3

Helix

362 – 379

18

Sequences

	Sequence		Length	Mass (Da)
	Q9NXS2 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 2DCA79BED029DD4B	FASTA	382	42,924
	10 20 30 40 50 60 MRSGGRGRPR LRLGERGLME PLLPPKRRLL PRVRLLPLLL ALAVGSAFYT IWSGWHRRTE 70 80 90 100 110 120 ELPLGRELRV PLIGSLPEAR LRRVVGQLDP QRLWSTYLRP LLVVRTPGSP GNLQVRKFLE 130 140 150 160 170 180 ATLRSLTAGW HVELDPFTAS TPLGPVDFGN VVATLDPRAA RHLTLACHYD SKLFPPGSTP 190 200 210 220 230 240 FVGATDSAVP CALLLELAQA LDLELSRAKK QAAPVTLQLL FLDGEEALKE WGPKDSLYGS 250 260 270 280 290 300 RHLAQLMESI PHSPGPTRIQ AIELFMLLDL LGAPNPTFYS HFPRTVRWFH RLRSIEKRLH 310 320 330 340 350 360 RLNLLQSHPQ EVMYFQPGEP FGSVEDDHIP FLRRGVPVLH LISTPFPAVW HTPADTEVNL 370 380 HPPTVHNLCR ILAVFLAEYL GL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
[2]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum.
[3]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[5]	"Isolation of an isoenzyme of human glutaminyl cyclase: retention in the Golgi complex suggests involvement in the protein maturation machinery." Cynis H., Rahfeld J.U., Stephan A., Kehlen A., Koch B., Wermann M., Demuth H.U., Schilling S. J. Mol. Biol. 379:966-980(2008) [PubMed: 18486145] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
[6]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]	"Structures of human Golgi-resident glutaminyl cyclase and its complexes with inhibitors reveal a large loop movement upon inhibitor binding." Huang K.F., Liaw S.S., Huang W.L., Chia C.Y., Lo Y.C., Chen Y.L., Wang A.H. J. Biol. Chem. 286:12439-12449(2011) [PubMed: 21288892] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 53-382 IN COMPLEXES WITH SYNTHETIC INHIBITORS PBD150 AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, COFACTOR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK000091 mRNA. Translation: BAA90938.1.
AK172764 mRNA. Translation: BAD18747.1.
AK222636 mRNA. Translation: BAD96356.1.
AC007191 Genomic DNA. No translation available.
BC011553 mRNA. Translation: AAH11553.1.

IPI

IPI00014877.

RefSeq

NP_001156849.1. NM_001163377.1.
NP_060129.2. NM_017659.3.

UniGene

Hs.631556.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3PB4	X-ray	1.13	X	53-382	[»]
3PB6	X-ray	1.05	X	53-382	[»]
3PB7	X-ray	1.40	X	53-382	[»]
3PB8	X-ray	1.13	X	53-382	[»]
3PB9	X-ray	1.12	X	53-382	[»]

ProteinModelPortal

Q9NXS2.

SMR

Q9NXS2. Positions 70-382.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NXS2. 3 interactions.

STRING

Q9NXS2.

Protein family/group databases

MEROPS

M28.016.

Polymorphism databases

DMDM

296452875.

Proteomic databases

PRIDE

Q9NXS2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000012049; ENSP00000012049; ENSG00000011478.

GeneID

54814.

KEGG

hsa:54814.

UCSC

uc002pcx.1. human.

Organism-specific databases

CTD

54814.

GeneCards

GC19P046195.

HGNC

HGNC:25952. QPCTL.

HPA

HPA040797.

neXtProt

NX_Q9NXS2.

PharmGKB

PA134922163.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG18999.

GeneTree

ENSGT00390000003107.

HOGENOM

HBG314483.

HOVERGEN

HBG009812.

InParanoid

Q9NXS2.

OMA

DPQRLWG.

OrthoDB

EOG441QC0.

PhylomeDB

Q9NXS2.

Gene expression databases

ArrayExpress

Q9NXS2.

Bgee

Q9NXS2.

CleanEx

HS_QPCTL.

Genevestigator

Q9NXS2.

Family and domain databases

InterPro

IPR007484. Peptidase_M28.
[Graphical view]

Pfam

PF04389. Peptidase_M28. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

57549.

Entry information

Entry name

QPCTL_HUMAN

Accession

Primary (citable) accession number: Q9NXS2
Secondary accession number(s): Q53HE4, Q96F74

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	May 18, 2010
Last modified:	January 25, 2012
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.