P01034 (CYTC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cystatin-C

Alternative name(s):
Cystatin-3
Gamma-trace
Neuroendocrine basic polypeptide
Post-gamma-globulin

Gene names

Name:

CST3

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

General annotation (Comments)

Function	As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity.
Subunit structure	Homodimer.
Subcellular location	Secreted Ref.19.
Tissue specificity	Expressed in submandibular and sublingual saliva but not in parotid saliva (at protein level). Expressed in various body fluids, such as the cerebrospinal fluid and plasma. Expressed in highest levels in the epididymis, vas deferens, brain, thymus, and ovary and the lowest in the submandibular gland. Ref.16 Ref.19
Post-translational modification	The Thr-25 variant is O-glycosylated with a core 1 or possibly core 8 glycan. The signal peptide of the O-glycosylated Thr-25 variant is cleaved between Ala-20 and Val-21. Ref.18
Involvement in disease	Defects in CST3 are the cause of amyloidosis type 6 (AMYL6) [MIM:105150]; also known as hereditary cerebral hemorrhage with amyloidosis (HCHWA), cerebral amyloid angiopathy (CAA) or cerebroarterial amyloidosis Icelandic type. AMYL6 is a hereditary generalized amyloidosis due to cystatin C amyloid deposition. Cystatin C amyloid accumulates in the walls of arteries, arterioles, and sometimes capillaries and veins of the brain, and in various organs including lymphoid tissue, spleen, salivary glands, and seminal vesicles. Amyloid deposition in the cerebral vessels results in cerebral amyloid angiopathy, cerebral hemorrhage and premature stroke. Cystatin C levels in the cerebrospinal fluid are abnormally low. Ref.3 Ref.22 Genetic variations in CST3 are associated with age-related macular degeneration type 11 (ARMD11) [MIM:611953]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. Ref.23
Miscellaneous	Potential cerebrospinal fluid marker for the diagnosis of Creutzfeldt-Jakob disease.
Sequence similarities	Belongs to the cystatin family.
Mass spectrometry	Molecular mass is 13334.5829±0.0140 Da from positions 27 - 146. Determined by ESI. Ref.19

Ontologies

Keywords
Cellular component	Amyloid Secreted
Coding sequence diversity	Polymorphism
Disease	Age-related macular degeneration Amyloidosis Disease mutation
Domain	Signal
Molecular function	Protease inhibitor Thiol protease inhibitor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	defense response Inferred from direct assay. Source: BHF-UCL fibril organization Inferred from genetic interaction. Source: BHF-UCL negative regulation of blood vessel remodeling Inferred from expression pattern. Source: BHF-UCL negative regulation of collagen catabolic process Inferred from expression pattern. Source: BHF-UCL negative regulation of elastin catabolic process Inferred from mutant phenotype. Source: BHF-UCL negative regulation of extracellular matrix disassembly Inferred from expression pattern. Source: BHF-UCL negative regulation of histolysis Inferred by curator. Source: BHF-UCL
Cellular component	extracellular space Inferred from direct assay. Source: BHF-UCL
Molecular function	beta-amyloid binding Inferred from physical interaction. Source: BHF-UCL cysteine-type endopeptidase inhibitor activity Inferred from direct assay. Source: BHF-UCL protease binding Inferred from physical interaction. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Ref.11 Ref.12 Ref.13 Ref.14

Chain

27 – 146

120

Cystatin-C Ref.1 Ref.3

PRO_0000006639

Regions

Motif

81 – 85

5

Secondary area of contact

Sites

Site

37

1

Reactive site

Amino acid modifications

Disulfide bond

99 ↔ 109

Ref.15 Ref.19

Disulfide bond

123 ↔ 143

Ref.15 Ref.19

Natural variations

Natural variant

25

1

A → T Associated with ARMD11 and O-glycosylated in region between AA 22-28. Ref.2 Ref.18 Ref.23
Corresponds to variant rs1064039 [ dbSNP | Ensembl ].

VAR_011893

Natural variant

94

1

L → Q in AMYL6. Ref.3 Ref.22
Corresponds to variant rs28939068 [ dbSNP | Ensembl ].

VAR_002207

Experimental info

Mutagenesis

25

1

A → S: Shows a dual distribution to the Golgi apparatus and to the mitochondria. Ref.17

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

146

Helix Strand Turn

Details...

Helix

47 – 63

17

Beta strand

67 – 100

34

Helix

106 – 108

3

Turn

115 – 117

3

Beta strand

120 – 130

11

Helix

131 – 133

3

Beta strand

135 – 145

11

Sequences

	Sequence		Length	Mass (Da)
	P01034 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: 75EF049CAE2E8B2B	FASTA	146	15,799
	10 20 30 40 50 60 MAGPLRAPLL LLAILAVALA VSPAAGSSPG KPPRLVGGPM DASVEEEGVR RALDFAVGEY 70 80 90 100 110 120 NKASNDMYHS RALQVVRARK QIVAGVNYFL DVELGRTTCT KTQPNLDNCP FHDQPHLKRK 130 140 AFCSFQIYAV PWQGTMTLSK STCQDA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C." Abrahamson M., Grubb A., Olafsson I., Lundwall A. FEBS Lett. 216:229-233(1987) [PubMed: 3495457] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"The human cystatin C gene (CST3) is a member of the cystatin gene family which is localized on chromosome 20." Saitoh E., Sabatini L.M., Eddy R.L., Shows T.B., Azen E.A., Isemura S., Sanada K. Biochem. Biophys. Res. Commun. 162:1324-1331(1989) [PubMed: 2764935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-25.
[3]	"Stroke in Icelandic patients with hereditary amyloid angiopathy is related to a mutation in the cystatin C gene, an inhibitor of cysteine proteases." Levy E., Lopez-Otin C., Ghiso J., Geltner D., Frangione B. J. Exp. Med. 169:1771-1778(1989) [PubMed: 2541223] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT AMYL6 GLN-94. Tissue: Brain.
[4]	"Structure and expression of the human cystatin C gene." Abrahamson M., Olafsson I., Palsdottir A., Ulvsbaeck M., Lundwall A., Jensson O., Grubb A. Biochem. J. 268:287-294(1990) [PubMed: 2363674] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Leukocyte.
[5]	"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: Synovial cell.
[6]	"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].
[7]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	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].
[10]	"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: Brain.
[11]	"Human gamma-trace, a basic microprotein: amino acid sequence and presence in the adenohypophysis." Grubb A., Loefberg H. Proc. Natl. Acad. Sci. U.S.A. 79:3024-3027(1982) [PubMed: 6283552] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-146.
[12]	"Human cystatin, a new protein inhibitor of cysteine proteinases." Brzin J., Popovic T., Turk V. Biochem. Biophys. Res. Commun. 118:103-109(1984) [PubMed: 6365094] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-76.
[13]	"Protein inhibitors of cysteine proteinases. III. Amino-acid sequence of cystatin from chicken egg white." Turk V., Brzin J., Longer M., Ritonja A., Eropkin M., Borchart U., Machleidt W. Hoppe-Seyler's Z. Physiol. Chem. 364:1487-1496(1983) [PubMed: 6662498] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-73.
[14]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-41.
[15]	"The disulphide bridges of human cystatin C (gamma-trace) and chicken cystatin." Grubb A., Loefberg H., Barrett A.J. FEBS Lett. 170:370-374(1984) Cited for: DISULFIDE BONDS.
[16]	"Cystatin C as a potential cerebrospinal fluid marker for the diagnosis of Creutzfeldt-Jakob disease." Sanchez J.C., Guillaume E., Lescuyer P., Allard L., Carrette O., Scherl A., Burgess J., Corthals G.L., Burkhard P.R., Hochstrasser D.F. Proteomics 4:2229-2233(2004) [PubMed: 15274116] [Abstract] Cited for: TISSUE SPECIFICITY.
[17]	"A dual Golgi- and mitochondria-localised Ala25Ser precursor cystatin C: an additional tool for characterising intracellular mis-localisation leading to increased AMD susceptibility." Ratnayaka A., Paraoan L., Spiller D.G., Hiscott P., Nelson G., White M.R., Grierson I. Exp. Eye Res. 84:1135-1139(2007) [PubMed: 16635487] [Abstract] Cited for: MUTAGENESIS OF ALA-25.
[18]	"Enrichment of glycopeptides for glycan structure and attachment site identification." Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G. Nat. Methods 6:809-811(2009) [PubMed: 19838169] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS], STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY, CHARACTERIZATION OF VARIANT THR-25. Tissue: Cerebrospinal fluid.
[19]	"Confident assignment of intact mass tags to human salivary cystatins using top-down Fourier-transform ion cyclotron resonance mass spectrometry." Ryan C.M., Souda P., Halgand F., Wong D.T., Loo J.A., Faull K.F., Whitelegge J.P. J. Am. Soc. Mass Spectrom. 21:908-917(2010) [PubMed: 20189825] [Abstract] Cited for: DISULFIDE BONDS, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MASS SPECTROMETRY. Tissue: Saliva.
[20]	"Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping." Janowski R., Kozak M., Jankowska E., Grzonka Z., Grubb A., Abrahamson M., Jaskolski M. Nat. Struct. Biol. 8:316-320(2001) [PubMed: 11276250] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-146.
[21]	"3D domain-swapped human cystatin C with amyloid-like intermolecular beta-sheets." Janowski R., Kozak M., Abrahamson M., Grubb A., Jaskolski M. Proteins 61:570-578(2005) [PubMed: 16170782] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.03 ANGSTROMS) OF 27-146.
[22]	"Hereditary cystatin C amyloid angiopathy: identification of the disease-causing mutation and specific diagnosis by polymerase chain reaction based analysis." Abrahamson M., Jonsdottir S., Olafsson I., Jensson O., Grubb A. Hum. Genet. 89:377-380(1992) [PubMed: 1352269] [Abstract] Cited for: VARIANT AMYL6 GLN-94.
[23]	"CST3 genotype associated with exudative age related macular degeneration." Zurdel J., Finckh U., Menzer G., Nitsch R.M., Richard G. Br. J. Ophthalmol. 86:214-219(2002) [PubMed: 11815350] [Abstract] Cited for: ASSOCIATION OF VARIANT THR-25 WITH ARMD11.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X05607 mRNA. Translation: CAA29096.1.
M27891, M27889, M27890 Genomic DNA. Translation: AAA52164.1.
X61681, X61682, X61683 Genomic DNA. Translation: CAA43856.2.
X52255 Genomic DNA. Translation: CAA36497.1.
AK312213 mRNA. Translation: BAG35146.1.
BT006839 mRNA. Translation: AAP35485.1.
CR541988 mRNA. Translation: CAG46785.1.
CR542018 mRNA. Translation: CAG46815.1.
AL121894 Genomic DNA. Translation: CAC05424.1.
CH471133 Genomic DNA. Translation: EAX10137.1.
CH471133 Genomic DNA. Translation: EAX10138.1.
BC013083 mRNA. Translation: AAH13083.1.
BC110305 mRNA. Translation: AAI10306.1.

IPI

IPI00032293.

PIR

UDHU. S10216.

RefSeq

NP_000090.1. NM_000099.2.

UniGene

Hs.304682.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G96	X-ray	2.50	A	27-146	[»]
1R4C	X-ray	2.18	A/B/C/D/E/F/G/H	37-146	[»]
1TIJ	X-ray	3.03	A/B	27-146	[»]
3GAX	X-ray	1.70	A/B	27-146	[»]
3NX0	X-ray	2.04	A/B	27-146	[»]

ProteinModelPortal

P01034.

SMR

P01034. Positions 36-146.

ModBase

Search...

Protein-protein interaction databases

IntAct

P01034. 4 interactions.

MINT

MINT-2857857.

STRING

P01034.

Protein family/group databases

MEROPS

I25.004.

Polymorphism databases

DMDM

118183.

2D gel databases

DOSAC-COBS-2DPAGE

P01034.

UCD-2DPAGE

P01034.

Proteomic databases

PeptideAtlas

P01034.

PRIDE

P01034.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000376925; ENSP00000366124; ENSG00000101439.
ENST00000398409; ENSP00000381446; ENSG00000101439.
ENST00000398411; ENSP00000381448; ENSG00000101439.

GeneID

1471.

KEGG

hsa:1471.

UCSC

uc002wtm.2. human.

Organism-specific databases

CTD

1471.

GeneCards

GC20M023608.

H-InvDB

HIX0015694.

HGNC

HGNC:2475. CST3.

HPA

CAB000118.
HPA013143.

MIM

105150. phenotype.
604312. gene.
611953. phenotype.

neXtProt

NX_P01034.

Orphanet

85458. Hereditary cerebral hemorrhage with amyloidosis.

PharmGKB

PA26976.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20133.

GeneTree

ENSGT00570000079039.

HOGENOM

HBG717109.

HOVERGEN

HBG009556.

InParanoid

P01034.

OMA

ASNDAYH.

OrthoDB

EOG49GKJ0.

PhylomeDB

P01034.

Enzyme and pathway databases

Reactome

REACT_75925. Amyloids.

Gene expression databases

ArrayExpress

P01034.

Bgee

P01034.

CleanEx

HS_CST3.

Genevestigator

P01034.

GermOnline

ENSG00000101439. Homo sapiens.

Family and domain databases

InterPro

IPR000010. Prot_inh_cystat.
IPR018073. Prot_inh_cystat_CS.
[Graphical view]

KO

K13899.

Pfam

PF00031. Cystatin. 1 hit.
[Graphical view]

SMART

SM00043. CY. 1 hit.
[Graphical view]

PROSITE

PS00287. CYSTATIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

6039.

PMAP-CutDB

P01034.

SOURCE

Search...

Entry information

Entry name

CYTC_HUMAN

Accession

Primary (citable) accession number: P01034
Secondary accession number(s): B2R5J9, D3DW42, Q6FGW9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 1, 1988
Last modified:	January 25, 2012
This is version 145 of the entry and version 1 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.