P32321 (DCTD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Deoxycytidylate deaminase
EC=3.5.4.12

Alternative name(s):
dCMP deaminase

Gene names

Name:

DCTD

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	178 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Supplies the nucleotide substrate for thymidylate synthetase.
Catalytic activity	dCMP + H2O = dUMP + NH3.
Cofactor	Zinc.
Enzyme regulation	Allosteric enzyme whose activity is greatly influenced by the end products of its metabolic pathway, dCTP and dTTP.
Subunit structure	Homohexamer.
Sequence similarities	Belongs to the cytidine and deoxycytidylate deaminase family.

Ontologies

Keywords
Biological process	Nucleotide biosynthesis
Coding sequence diversity	Alternative splicing
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW pyrimidine nucleobase metabolic process Traceable author statement. Source: Reactome pyrimidine nucleoside biosynthetic process Traceable author statement. Source: Reactome pyrimidine nucleotide metabolic process Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	dCMP deaminase activity Inferred from experiment. Source: Reactome zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P32321-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P32321-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVGGGQPCGPNM

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 178

178

Deoxycytidylate deaminase

PRO_0000171691

Sites

Active site

86

1

Proton donor By similarity

Metal binding

84

1

Zinc; catalytic By similarity

Metal binding

110

1

Zinc; catalytic By similarity

Metal binding

113

1

Zinc; catalytic By similarity

Natural variations

Alternative sequence

1

1

M → MVGGGQPCGPNM in isoform 2.

VSP_038094

Experimental info

Sequence conflict

95

1

S → L in AAH01286. Ref.6

Sequence conflict

128

1

M → T in AAA35755. Ref.1

Secondary structure

1

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178

Helix Strand Turn

Details...

Helix

15 – 27

13

Beta strand

38 – 42

5

Beta strand

48 – 55

8

Turn

62 – 64

3

Helix

74 – 76

3

Turn

79 – 81

3

Helix

85 – 91

7

Beta strand

102 – 107

6

Helix

111 – 119

9

Beta strand

124 – 129

6

Turn

131 – 134

4

Helix

136 – 148

13

Beta strand

151 – 154

4

Beta strand

160 – 165

6

Helix

166 – 168

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 19, 2002. Version 2. Checksum: 2B8DA5EAC85F3666	FASTA	178	20,016
	10 20 30 40 50 60 MSEVSCKKRD DYLEWPEYFM AVAFLSAQRS KDPNSQVGAC IVNSENKIVG IGYNGMPNGC 70 80 90 100 110 120 SDDVLPWRRT AENKLDTKYP YVCHAELNAI MNKNSTDVKG CSMYVALFPC NECAKLIIQA 130 140 150 160 170 GIKEVIFMSD KYHDSDEATA ARLLFNMAGV TFRKFIPKCS KIVIDFDSIN SRPSQKLQ
	Isoform 2 [UniParc]. Checksum: 973677A3294EBB97	FASTA	189	21,014
	10 20 30 40 50 60 MVGGGQPCGP NMSEVSCKKR DDYLEWPEYF MAVAFLSAQR SKDPNSQVGA CIVNSENKIV 70 80 90 100 110 120 GIGYNGMPNG CSDDVLPWRR TAENKLDTKY PYVCHAELNA IMNKNSTDVK GCSMYVALFP 130 140 150 160 170 180 CNECAKLIIQ AGIKEVIFMS DKYHDSDEAT AARLLFNMAG VTFRKFIPKC SKIVIDFDSI NSRPSQKLQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of human deoxycytidylate deaminase and overexpression of its functional protein in Escherichia coli." Weiner K.X., Weiner R.S., Maley F., Maley G.F. J. Biol. Chem. 268:12983-12989(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[2]	"Chromosomal location and structural organization of the human deoxycytidylate deaminase gene." Weiner K.X., Ciesla J., Jaffe A.B., Ketring R., Maley F., Maley G.F. J. Biol. Chem. 270:18727-18729(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Lung.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Cervix and Testis.
[7]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L12136 mRNA. Translation: AAA35755.1.
L39874 Genomic DNA. Translation: AAC37579.1.
AK313221 mRNA. Translation: BAG36033.1.
AC079766 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04697.1.
CH471056 Genomic DNA. Translation: EAX04698.1.
CH471056 Genomic DNA. Translation: EAX04700.1.
CH471056 Genomic DNA. Translation: EAX04701.1.
BC001286 mRNA. Translation: AAH01286.1.
BC088357 mRNA. Translation: AAH88357.2.

IPI

IPI00296863.
IPI00554705.

PIR

A47288.
I55434.

RefSeq

NP_001012750.1. NM_001012732.1.
NP_001912.2. NM_001921.2.

UniGene

Hs.183850.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2W4L	X-ray	2.10	A/B/C/D/E/F	5-173	[»]

ProteinModelPortal

P32321.

ModBase

Search...

Protein-protein interaction databases

IntAct

P32321. 4 interactions.

MINT

MINT-3013156.

STRING

9606.ENSP00000349576.

PTM databases

PhosphoSite

P32321.

Polymorphism databases

DMDM

23503055.

Proteomic databases

PaxDb

P32321.

PRIDE

P32321.

Protocols and materials databases

DNASU

1635.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000357067; ENSP00000349576; ENSG00000129187.
ENST00000438320; ENSP00000398194; ENSG00000129187.
ENST00000510370; ENSP00000424017; ENSG00000129187.

GeneID

1635.

KEGG

hsa:1635.

UCSC

uc003ivf.3. human.
uc003ivg.3. human.

Organism-specific databases

CTD

1635.

GeneCards

GC04M183811.

HGNC

HGNC:2710. DCTD.

HPA

HPA035894.

MIM

607638. gene.

neXtProt

NX_P32321.

PharmGKB

PA138.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2131.

HOGENOM

HOG000015715.

HOVERGEN

HBG025823.

InParanoid

P32321.

KO

K01493.

OMA

DYISWDE.

OrthoDB

EOG45B1GM.

PhylomeDB

P32321.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

P32321.

Gene expression databases

ArrayExpress

P32321.

Bgee

P32321.

CleanEx

HS_DCTD.

Genevestigator

P32321.

GermOnline

ENSG00000129187. Homo sapiens.

Family and domain databases

InterPro

IPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR015517. Cyt_deaminase.
IPR016193. Cytidine_deaminase-like.
IPR016473. dCMP_deaminase.
[Graphical view]

PANTHER

PTHR11086. PTHR11086. 1 hit.

Pfam

PF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]

PIRSF

PIRSF006019. dCMP_deaminase. 1 hit.

SUPFAM

SSF53927. Cytidine_deaminase-like. 1 hit.

PROSITE

PS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL5675.

ChiTaRS

DCTD. human.

EvolutionaryTrace

P32321.

GenomeRNAi

1635.

NextBio

6716.

SOURCE

Search...

Entry information

Entry name

DCTD_HUMAN

Accession

Primary (citable) accession number: P32321
Secondary accession number(s): B2R836 , D3DP49, D3DP50, Q5M7Z8, Q9BVD8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	September 19, 2002
Last modified:	May 1, 2013
This is version 125 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.