P12955 (PEPD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Xaa-Pro dipeptidase
Short name=X-Pro dipeptidase
EC=3.4.13.9

Alternative name(s):
Imidodipeptidase
Peptidase D
Proline dipeptidase
Short name=Prolidase

Gene names

Name:	PEPD
Synonyms:	PRD

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	493 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen.
Catalytic activity	Hydrolysis of Xaa-|-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.
Cofactor	Binds 2 manganese ions per subunit. Ref.8
Subunit structure	Homodimer.
Involvement in disease	Prolidase deficiency (PD) [MIM:170100]: A multisystem disorder associated with massive iminodipeptiduria and lack of or reduced prolidase activity in erythrocytes, leukocytes, or cultured fibroblasts. Clinical features include skin ulcers, developmental delay, recurrent infections, and a characteristic facies. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10 Ref.11 Ref.12
Sequence similarities	Belongs to the peptidase M24B family. Eukaryotic-type prolidase subfamily.
Mass spectrometry	Molecular mass is 54251.73 Da from positions 2 - 493. Determined by MALDI. Ref.6

Ontologies

Keywords
Biological process	Collagen degradation
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Ligand	Manganese Metal-binding
Molecular function	Dipeptidase Hydrolase Metalloprotease Protease
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular amino acid metabolic process Traceable author statement PubMed 1972707. Source: ProtInc collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Traceable author statement PubMed 1972707. Source: ProtInc
Molecular_function	aminopeptidase activity Inferred from electronic annotation. Source: InterPro dipeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: InterPro metallocarboxypeptidase activity Traceable author statement PubMed 1972707. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P12955-1)

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: P12955-2)

The sequence of this isoform differs from the canonical sequence as follows:
     184-224: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: P12955-3)

The sequence of this isoform differs from the canonical sequence as follows:
     68-131: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 493

493

Xaa-Pro dipeptidase

PRO_0000185087

Sites

Metal binding

276

1

Manganese 1

Metal binding

287

1

Manganese 1

Metal binding

287

1

Manganese 2

Metal binding

370

1

Manganese 2

Metal binding

412

1

Manganese 2

Metal binding

452

1

Manganese 1

Metal binding

452

1

Manganese 2

Natural variations

Alternative sequence

68 – 131

64

Missing in isoform 3.

VSP_045370

Alternative sequence

184 – 224

41

Missing in isoform 2.

VSP_042629

Natural variant

184

1

R → Q in PD. Ref.11

VAR_011614

Natural variant

276

1

D → N in PD. Ref.9

VAR_004404

Natural variant

278

1

G → D in PD. Ref.11

VAR_011615

Natural variant

388

1

R → H.
Corresponds to variant rs2230062 [ dbSNP | Ensembl ].

VAR_051574

Natural variant

435

1

L → F. Ref.3 Ref.5
Corresponds to variant rs17570 [ dbSNP | Ensembl ].

VAR_014723

Natural variant

448

1

G → R in PD. Ref.10 Ref.11 Ref.12

VAR_004405

Natural variant

452

1

Missing in PD. Ref.10 Ref.11

VAR_004406

Experimental info

Sequence conflict

48

1

L → R in BAF84250. Ref.3

Sequence conflict

66

1

R → L in AAA60064. Ref.1

Sequence conflict

107

1

W → R in BAF83470. Ref.3

Sequence conflict

108

1

M → I in BAF83445. Ref.3

Sequence conflict

183

1

C → S in AAA60064. Ref.1

Sequence conflict

221

1

E → G in AAA60064. Ref.1

Sequence conflict

283 – 284

2

CF → SV in AAA60064. Ref.1

Sequence conflict

294

1

A → R in AAA60064. Ref.1

Sequence conflict

311

1

R → L in AAA60064. Ref.1

Sequence conflict

324

1

V → D in AAA60064. Ref.1

Sequence conflict

329 – 330

2

MH → ID in AAA60064. Ref.1

Sequence conflict

408

1

V → A in BAG56678. Ref.3

Sequence conflict

458

1

T → I in AAA60064. Ref.1

Sequence conflict

478

1

C → R in BAF83470. Ref.3

Secondary structure

1

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493

Helix Strand Turn

Details...

Helix

21 – 36

16

Beta strand

45 – 49

5

Beta strand

54 – 56

3

Helix

69 – 75

7

Beta strand

79 – 81

3

Beta strand

83 – 87

5

Turn

88 – 90

3

Beta strand

93 – 97

5

Helix

102 – 104

3

Turn

105 – 107

3

Helix

114 – 121

8

Beta strand

124 – 128

5

Helix

129 – 131

3

Helix

132 – 138

7

Turn

152 – 154

3

Helix

166 – 168

3

Helix

176 – 185

10

Helix

189 – 212

24

Helix

219 – 234

16

Beta strand

238 – 241

4

Beta strand

244 – 247

4

Helix

248 – 252

5

Beta strand

272 – 277

6

Beta strand

279 – 281

3

Beta strand

288 – 293

6

Helix

300 – 319

20

Helix

326 – 343

18

Helix

351 – 356

6

Turn

357 – 359

3

Helix

360 – 363

4

Beta strand

373 – 377

5

Helix

394 – 396

3

Beta strand

408 – 411

4

Beta strand

414 – 416

3

Helix

419 – 427

9

Helix

429 – 432

4

Helix

437 – 443

7

Beta strand

448 – 450

3

Beta strand

452 – 457

6

Beta strand

459 – 464

6

Helix

472 – 479

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E8C4A2497E44BA22	FASTA	493	54,548
	10 20 30 40 50 60 MAAATGPSFW LGNETLKVPL ALFALNRQRL CERLRKNPAV QAGSIVVLQG GEETQRYCTD 70 80 90 100 110 120 TGVLFRQESF FHWAFGVTEP GCYGVIDVDT GKSTLFVPRL PASHATWMGK IHSKEHFKEK 130 140 150 160 170 180 YAVDDVQYVD EIASVLTSQK PSVLLTLRGV NTDSGSVCRE ASFDGISKFE VNNTILHPEI 190 200 210 220 230 240 VECRVFKTDM ELEVLRYTNK ISSEAHREVM KAVKVGMKEY ELESLFEHYC YSRGGMRHSS 250 260 270 280 290 300 YTCICGSGEN SAVLHYGHAG APNDRTIQNG DMCLFDMGGE YYCFASDITC SFPANGKFTA 310 320 330 340 350 360 DQKAVYEAVL RSSRAVMGAM KPGVWWPDMH RLADRIHLEE LAHMGILSGS VDAMVQAHLG 370 380 390 400 410 420 AVFMPHGLGH FLGIDVHDVG GYPEGVERID EPGLRSLRTA RHLQPGMVLT VEPGIYFIDH 430 440 450 460 470 480 LLDEALADPA RASFLNREVL QRFRGFGGVR IEEDVVVTDS GIELLTCVPR TVEEIEACMA 490 GCDKAFTPFS GPK
	Isoform 2 [UniParc]. Checksum: EA1B0DFBE694A180	FASTA	452	49,691
	10 20 30 40 50 60 MAAATGPSFW LGNETLKVPL ALFALNRQRL CERLRKNPAV QAGSIVVLQG GEETQRYCTD 70 80 90 100 110 120 TGVLFRQESF FHWAFGVTEP GCYGVIDVDT GKSTLFVPRL PASHATWMGK IHSKEHFKEK 130 140 150 160 170 180 YAVDDVQYVD EIASVLTSQK PSVLLTLRGV NTDSGSVCRE ASFDGISKFE VNNTILHPEI 190 200 210 220 230 240 VECLFEHYCY SRGGMRHSSY TCICGSGENS AVLHYGHAGA PNDRTIQNGD MCLFDMGGEY 250 260 270 280 290 300 YCFASDITCS FPANGKFTAD QKAVYEAVLR SSRAVMGAMK PGVWWPDMHR LADRIHLEEL 310 320 330 340 350 360 AHMGILSGSV DAMVQAHLGA VFMPHGLGHF LGIDVHDVGG YPEGVERIDE PGLRSLRTAR 370 380 390 400 410 420 HLQPGMVLTV EPGIYFIDHL LDEALADPAR ASFLNREVLQ RFRGFGGVRI EEDVVVTDSG 430 440 450 IELLTCVPRT VEEIEACMAG CDKAFTPFSG PK
	Isoform 3 [UniParc]. Checksum: 2D094B4069E39CF5	FASTA	429	47,261
	10 20 30 40 50 60 MAAATGPSFW LGNETLKVPL ALFALNRQRL CERLRKNPAV QAGSIVVLQG GEETQRYCTD 70 80 90 100 110 120 TGVLFRQIAS VLTSQKPSVL LTLRGVNTDS GSVCREASFD GISKFEVNNT ILHPEIVECR 130 140 150 160 170 180 VFKTDMELEV LRYTNKISSE AHREVMKAVK VGMKEYELES LFEHYCYSRG GMRHSSYTCI 190 200 210 220 230 240 CGSGENSAVL HYGHAGAPND RTIQNGDMCL FDMGGEYYCF ASDITCSFPA NGKFTADQKA 250 260 270 280 290 300 VYEAVLRSSR AVMGAMKPGV WWPDMHRLAD RIHLEELAHM GILSGSVDAM VQAHLGAVFM 310 320 330 340 350 360 PHGLGHFLGI DVHDVGGYPE GVERIDEPGL RSLRTARHLQ PGMVLTVEPG IYFIDHLLDE 370 380 390 400 410 420 ALADPARASF LNREVLQRFR GFGGVRIEED VVVTDSGIEL LTCVPRTVEE IEACMAGCDK AFTPFSGPK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure and gene localization of human prolidase." Endo F., Tanoue A., Nakai H., Hata A., Indo Y., Titani K., Matsuda I. J. Biol. Chem. 264:4476-4481(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE. Tissue: Liver and Placenta.
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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] (ISOFORMS 1; 2 AND 3), VARIANT PHE-435. Tissue: Brain and Kidney.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORM 1), VARIANT PHE-435. Tissue: Kidney, Skin and Uterus.
[6]	"Cluster analysis of an extensive human breast cancer cell line protein expression map database." Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J. Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY. Tissue: Mammary cancer.
[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].
[8]	"Crystal structure of human prolidase: the molecular basis of PD disease." Protein structure factory (PSF) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS, COFACTOR.
[9]	"A single nucleotide change in the prolidase gene in fibroblasts from two patients with polypeptide positive prolidase deficiency. Expression of the mutant enzyme in NIH 3T3 cells." Tanoue A., Endo F., Kitano A., Matsuda I. J. Clin. Invest. 86:351-355(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PD ASN-276.
[10]	"Four novel PEPD alleles causing prolidase deficiency." Ledoux P., Scriver C.R., Hechtman P. Am. J. Hum. Genet. 54:1014-1021(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PD ARG-448 AND GLU-452 DEL.
[11]	"Expression and molecular analysis of mutations in prolidase deficiency." Ledoux P., Scriver C.R., Hechtman P. Am. J. Hum. Genet. 59:1035-1039(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PD GLN-184; ASP-278; ARG-448 AND GLU-452 DEL.
[12]	"Mutation analysis of five new patients affected by prolidase deficiency: the lack of enzyme activity causes necrosis-like cell death in cultured fibroblasts." Forlino A., Lupi A., Vaghi P., Icaro Cornaglia A., Calligaro A., Campari E., Cetta G. Hum. Genet. 111:314-322(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PD ARG-448.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J04605 mRNA. Translation: AAA60064.1.
BT006692 mRNA. Translation: AAP35338.1.
AK290756 mRNA. Translation: BAF83445.1.
AK290781 mRNA. Translation: BAF83470.1.
AK291561 mRNA. Translation: BAF84250.1.
AK293126 mRNA. Translation: BAG56678.1.
AK294619 mRNA. Translation: BAG57802.1.
AC008744 Genomic DNA. No translation available.
AC010485 Genomic DNA. No translation available.
BC004305 mRNA. Translation: AAH04305.1.
BC015027 mRNA. Translation: AAH15027.1.
BC028295 mRNA. Translation: AAH28295.1.

IPI

IPI00257882.
IPI00909399.
IPI00910514.

PIR

A32454.

RefSeq

NP_000276.2. NM_000285.3.
NP_001159528.1. NM_001166056.1.
NP_001159529.1. NM_001166057.1.

UniGene

Hs.36473.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IW2	X-ray	1.82	A/B	2-492	[»]
2OKN	X-ray	2.45	A/B	2-492	[»]

ProteinModelPortal

P12955.

ModBase

Search...

Protein-protein interaction databases

IntAct

P12955. 8 interactions.

MINT

MINT-5000488.

STRING

9606.ENSP00000244137.

Protein family/group databases

MEROPS

M24.007.

PTM databases

PhosphoSite

P12955.

Polymorphism databases

DMDM

50403718.

2D gel databases

REPRODUCTION-2DPAGE

IPI00257882.

Proteomic databases

PaxDb

P12955.

PeptideAtlas

P12955.

PRIDE

P12955.

Protocols and materials databases

DNASU

5184.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000244137; ENSP00000244137; ENSG00000124299.
ENST00000397032; ENSP00000380226; ENSG00000124299.
ENST00000436370; ENSP00000391890; ENSG00000124299.

GeneID

5184.

KEGG

hsa:5184.

UCSC

uc002nur.4. human.

Organism-specific databases

CTD

5184.

GeneCards

GC19M033877.

HGNC

HGNC:8840. PEPD.

HPA

HPA015599.

MIM

170100. phenotype.
613230. gene.

neXtProt

NX_P12955.

Orphanet

742. Prolidase deficiency.

PharmGKB

PA33181.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0006.

HOGENOM

HOG000008763.

HOVERGEN

HBG053562.

InParanoid

P12955.

KO

K14213.

OMA

ITIEPGC.

PhylomeDB

P12955.

Gene expression databases

ArrayExpress

P12955.

Bgee

P12955.

CleanEx

HS_PEPD.

Genevestigator

P12955.

GermOnline

ENSG00000124299. Homo sapiens.

Family and domain databases

Gene3D

3.90.230.10. 1 hit.

InterPro

IPR007865. Aminopep_P_N.
IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
[Graphical view]

Pfam

PF05195. AMP_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view]

SMART

SM01011. AMP_N. 1 hit.
[Graphical view]

SUPFAM

SSF55920. Peptidase_M24_cat_core. 1 hit.

PROSITE

PS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P12955.

ChEMBL

CHEMBL4185.

ChiTaRS

PEPD. human.

EvolutionaryTrace

P12955.

GenomeRNAi

5184.

NextBio

20054.

SOURCE

Search...

Entry information

Entry name

PEPD_HUMAN

Accession

Primary (citable) accession number: P12955
Secondary accession number(s): A8K3Z1 , A8K416, A8K696, A8MX47, B4DDB7, B4DGJ1, E9PCE8, Q8TBN9, Q9BT75

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 158 of the entry and version 3 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.