Q9NRA2 (S17A5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sialin

Alternative name(s):
H(+)/nitrate cotransporter
H(+)/sialic acid cotransporter
Short name=AST
Membrane glycoprotein HP59
Solute carrier family 17 member 5
Vesicular H(+)/Aspartate-glutamate cotransporter

Gene names

Name:

SLC17A5

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

General annotation (Comments)

Function	Transports glucuronic acid and free sialic acid out of the lysosome after it is cleaved from sialoglycoconjugates undergoing degradation, this is required for normal CNS myelination. Mediates aspartate and glutamate membrane potential-dependent uptake into synaptic vesicles and synaptic-like microvesicles. Also functions as an electrogenic 2NO3-/H+ cotransporter in the plasma membrane of salivary gland acinar cells, mediating the physiological nitrate efflux, 25% of the circulating nitrate ions is typically removed and secreted in saliva. Ref.1 Ref.2 Ref.6 Ref.9 Ref.10
Subcellular location	Cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle › secretory vesicle › synaptic vesicle membrane. Lysosome membrane; Multi-pass membrane protein Ref.7 Ref.9 Ref.10.
Tissue specificity	Found in fetal lung and small intestine, and at lower level in fetal skin and muscle. In the adult, detected in placenta, kidney and pancreas. Abundant in the endothelial cells of tumors from ovary, colon, breast and lung, but is not detected in endothelial cells from the corresponding normal tissues. Ref.1 Ref.2
Involvement in disease	Salla disease (SD) [MIM:604369]: Sialic acid storage disease (SASD). SASDs are autosomal recessive neurodegenerative disorders characterized by hypotonia, cerebellar ataxia and mental retardation. They are caused by a defect in the metabolism of sialic acid which results in increased urinary excretion of unconjugated sialic acid, specifically N-acetylneuraminic acid. Enlarged lysosomes are seen on electron microscopic studies. Clinical symptoms of SD present usually at age less than 1 year and progression is slow. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.9 Ref.11 Ref.12 Infantile sialic acid storage disorder (ISSD) [MIM:269920]: Severe form of sialic acid storage disease. Affected newborns exhibit visceromegaly, coarse features and failure to thrive immediately after birth. These patients have a shortened life span, usually less than 2 years. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.11 Infantile sialic acid storage disorder is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non-immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders.
Sequence similarities	Belongs to the major facilitator superfamily. Sodium/anion cotransporter family.
Sequence caution	The sequence AAF97769.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Amino-acid transport Symport Transport
Cellular component	Cell junction Cell membrane Cytoplasmic vesicle Lysosome Membrane Synapse
Coding sequence diversity	Alternative splicing
Disease	Disease mutation
Domain	Transmembrane Transmembrane helix
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	amino acid transport Inferred from electronic annotation. Source: UniProtKB-KW sialic acid transport Inferred from direct assay Ref.2. Source: MGI
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW integral to plasma membrane Traceable author statement Ref.2. Source: ProtInc lysosomal membrane Inferred from direct assay PubMed 3961501. Source: MGI synaptic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	sialic acid transmembrane transporter activity Inferred from direct assay Ref.2. Source: MGI sugar:hydrogen symporter activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9NRA2-1)

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: Q9NRA2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     274-276: LSS → AGV
     278-495: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 495	495	Sialin		PRO_0000220947
Regions
	Topological domain	1 – 41	41	Cytoplasmic Potential
	Transmembrane	42 – 62	21	Helical; Potential
	Topological domain	63 – 109	47	Lumenal Potential
	Transmembrane	110 – 130	21	Helical; Potential
	Topological domain	131 – 136	6	Cytoplasmic Potential
	Transmembrane	137 – 157	21	Helical; Potential
	Topological domain	158	1	Lumenal Potential
	Transmembrane	159 – 179	21	Helical; Potential
	Topological domain	180 – 200	21	Cytoplasmic Potential
	Transmembrane	201 – 221	21	Helical; Potential
	Topological domain	222 – 227	6	Lumenal Potential
	Transmembrane	228 – 248	21	Helical; Potential
	Topological domain	249 – 279	31	Cytoplasmic Potential
	Transmembrane	280 – 300	21	Helical; Potential
	Topological domain	301 – 328	28	Lumenal Potential
	Transmembrane	329 – 349	21	Helical; Potential
	Topological domain	350 – 365	16	Cytoplasmic Potential
	Transmembrane	366 – 386	21	Helical; Potential
	Topological domain	387 – 391	5	Lumenal Potential
	Transmembrane	392 – 412	21	Helical; Potential
	Topological domain	413 – 423	11	Cytoplasmic Potential
	Transmembrane	424 – 444	21	Helical; Potential
	Topological domain	445 – 457	13	Lumenal Potential
	Transmembrane	458 – 478	21	Helical; Potential
	Topological domain	479 – 495	17	Cytoplasmic Potential
	Motif	22 – 23	2	Dileucine internalization motif
Amino acid modifications
	Glycosylation	71	1	N-linked (GlcNAc...) Potential
	Glycosylation	77	1	N-linked (GlcNAc...) Potential
	Glycosylation	95	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	274 – 276	3	LSS → AGV in isoform 2.		VSP_010482
	Alternative sequence	278 – 495	218	Missing in isoform 2.		VSP_010483
	Natural variant	39	1	R → C in SD; completely devoid of aspartate and glutamate transport activity, but retains appreciable H(+)/sialic acid cotransport activity, frequent mutation in Finland. Ref.2 Ref.9 Ref.11 Ref.12		VAR_018684
	Natural variant	136	1	K → E in SD. Ref.11		VAR_018685
	Natural variant	183	1	H → R in ISSD. Ref.2 Ref.11		VAR_018686
	Natural variant	268 – 272	5	Missing in ISSD.		VAR_018687
	Natural variant	296	1	V → I. Corresponds to variant rs16883930 [ dbSNP | Ensembl ].		VAR_034746
	Natural variant	334	1	P → R in ISSD. Ref.2 Ref.11		VAR_018688
	Natural variant	371	1	G → V in ISSD. Ref.11		VAR_018689
Experimental info
	Mutagenesis	22 – 23	2	LL → GG: Targeted to plasma membrane; sialic acid uptake strongly activated at acidic pH. Ref.6
	Mutagenesis	179	1	F → C: 15 fold increase in affinity for glucuronic acid. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 7, 2004. Version 2. Checksum: 5C6C154B3E93A19E	FASTA	495	54,640
	10 20 30 40 50 60 MRSPVRDLAR NDGEESTDRT PLLPGAPRAE AAPVCCSARY NLAILAFFGF FIVYALRVNL 70 80 90 100 110 120 SVALVDMVDS NTTLEDNRTS KACPEHSAPI KVHHNQTGKK YQWDAETQGW ILGSFFYGYI 130 140 150 160 170 180 ITQIPGGYVA SKIGGKMLLG FGILGTAVLT LFTPIAADLG VGPLIVLRAL EGLGEGVTFP 190 200 210 220 230 240 AMHAMWSSWA PPLERSKLLS ISYAGAQLGT VISLPLSGII CYYMNWTYVF YFFGTIGIFW 250 260 270 280 290 300 FLLWIWLVSD TPQKHKRISH YEKEYILSSL RNQLSSQKSV PWVPILKSLP LWAIVVAHFS 310 320 330 340 350 360 YNWTFYTLLT LLPTYMKEIL RFNVQENGFL SSLPYLGSWL CMILSGQAAD NLRAKWNFST 370 380 390 400 410 420 LCVRRIFSLI GMIGPAVFLV AAGFIGCDYS LAVAFLTIST TLGGFCSSGF SINHLDIAPS 430 440 450 460 470 480 YAGILLGITN TFATIPGMVG PVIAKSLTPD NTVGEWQTVF YIAAAINVFG AIFFTLFAKG 490 EVQNWALNDH HGHRH
	Isoform 2 [UniParc]. Checksum: 1BF03EA560AB80DB	FASTA	277	30,667
	10 20 30 40 50 60 MRSPVRDLAR NDGEESTDRT PLLPGAPRAE AAPVCCSARY NLAILAFFGF FIVYALRVNL 70 80 90 100 110 120 SVALVDMVDS NTTLEDNRTS KACPEHSAPI KVHHNQTGKK YQWDAETQGW ILGSFFYGYI 130 140 150 160 170 180 ITQIPGGYVA SKIGGKMLLG FGILGTAVLT LFTPIAADLG VGPLIVLRAL EGLGEGVTFP 190 200 210 220 230 240 AMHAMWSSWA PPLERSKLLS ISYAGAQLGT VISLPLSGII CYYMNWTYVF YFFGTIGIFW 250 260 270 FLLWIWLVSD TPQKHKRISH YEKEYILSSL RNQAGVQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a novel membrane protein, HP59, with therapeutic potential as a target of tumor angiogenesis." Fu C., Bardhan S., Cetateanu N.D., Wamil B.D., Wang Y., Yan H.-P., Shi E., Carter C., Venkov C., Yakes F.M., Page D.L., Lloyd R.S., Mernaugh R.L., Hellerqvist C.G. Clin. Cancer Res. 7:4182-4194(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
[2]	"A new gene, encoding an anion transporter, is mutated in sialic acid storage diseases." Verheijen F.W., Verbeek E., Aula N., Beerens C.E.M.T., Havelaar A.C., Joosse M., Peltonen L., Aula P., Galjaard H., Van der Spek P.J., Mancini G.M.S. Nat. Genet. 23:462-465(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANT SD CYS-39, VARIANTS ISSD 268-SER--ASN-272 DEL; ARG-183 AND ARG-334.
[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 2).
[4]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [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 2). Tissue: Colon.
[6]	"Functional characterization of wild-type and mutant human sialin." Morin P., Sagne C., Gasnier B. EMBO J. 23:4560-4570(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DILEUCINE MOTIF, MUTAGENESIS OF 22-LEU--LEU-23.
[7]	"Integral and associated lysosomal membrane proteins." Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H., Elsaesser H.-P., Mann M., Hasilik A. Traffic 8:1676-1686(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Placenta.
[8]	"Structure-function studies of the SLC17 transporter sialin identify crucial residues and substrate-induced conformational changes." Courville P., Quick M., Reimer R.J. J. Biol. Chem. 285:19316-19323(2010) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY, MUTAGENESIS OF PHE-179.
[9]	"Functional characterization of vesicular excitatory amino acid transport by human sialin." Miyaji T., Omote H., Moriyama Y. J. Neurochem. 119:1-5(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, VARIANT SD CYS-39.
[10]	"Sialin (SLC17A5) functions as a nitrate transporter in the plasma membrane." Qin L., Liu X., Sun Q., Fan Z., Xia D., Ding G., Ong H.L., Adams D., Gahl W.A., Zheng C., Qi S., Jin L., Zhang C., Gu L., He J., Deng D., Ambudkar I.S., Wang S. Proc. Natl. Acad. Sci. U.S.A. 109:13434-13439(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]	"The spectrum of SLC17A5-gene mutations resulting in free sialic acid-storage diseases indicates some genotype-phenotype correlation." Aula N., Salomaeki P., Timonen R., Verheijen F., Mancini G.M.S., Maensson J.-E., Aula P., Peltonen L. Am. J. Hum. Genet. 67:832-840(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS SD CYS-39 AND GLU-136, VARIANTS ISSD 268-SER--ASN-272 DEL; ARG-183; ARG-334 AND VAL-371.
[12]	"Sialic acid storage disease of the Salla phenotype in American monozygous twin female sibs." Martin R.A., Slaugh R., Natowicz M., Pearlman K., Orvisky E., Krasnewich D., Kleta R., Huizing M., Gahl W.A. Am. J. Med. Genet. A 120:23-27(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SD CYS-39.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF244577 mRNA. Translation: AAF97769.1. Different initiation. AJ387747 mRNA. Translation: CAB62540.1. AK075320 mRNA. Translation: BAC11546.1. AL590428, AL121972 Genomic DNA. Translation: CAI15635.1. AL121972, AL590428 Genomic DNA. Translation: CAI20417.1. BC020961 mRNA. Translation: AAH20961.1.
IPI	IPI00395808. IPI00411564.
RefSeq	NP_036566.1. NM_012434.4.
UniGene	Hs.597422.
3D structure databases
ProteinModelPortal	Q9NRA2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NRA2. 1 interaction.
STRING	9606.ENSP00000348019.
Protein family/group databases
TCDB	2.A.1.14.10. major facilitator superfamily (MFS).
PTM databases
PhosphoSite	Q9NRA2.
Polymorphism databases
DMDM	48428688.
Proteomic databases
PaxDb	Q9NRA2.
PRIDE	Q9NRA2.
Protocols and materials databases
DNASU	26503.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000355773; ENSP00000348019; ENSG00000119899.
GeneID	26503.
KEGG	hsa:26503.
UCSC	uc003phn.4. human.
Organism-specific databases
CTD	26503.
GeneCards	GC06M074359.
HGNC	HGNC:10933. SLC17A5.
HPA	HPA044479.
MIM	269920. phenotype. 604322. gene. 604369. phenotype.
neXtProt	NX_Q9NRA2.
Orphanet	834. Free sialic acid storage disease.
PharmGKB	PA35824.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0477.
HOGENOM	HOG000230811.
HOVERGEN	HBG008834.
InParanoid	Q9NRA2.
KO	K12301.
OMA	SDYHGHR.
OrthoDB	EOG4640BQ.
PhylomeDB	Q9NRA2.
Enzyme and pathway databases
Reactome	REACT_15518. Transmembrane transport of small molecules. REACT_19419. Amino acid and oligopeptide SLC transporters.
Gene expression databases
ArrayExpress	Q9NRA2.
Bgee	Q9NRA2.
CleanEx	HS_SLC17A5.
Genevestigator	Q9NRA2.
GermOnline	ENSG00000119899. Homo sapiens.
Family and domain databases
InterPro	IPR011701. MFS. IPR020846. MFS_dom. IPR016196. MFS_dom_general_subst_transpt. [Graphical view]
Pfam	PF07690. MFS_1. 1 hit. [Graphical view]
SUPFAM	SSF103473. MFS_gen_substrate_transporter. 1 hit.
PROSITE	PS50850. MFS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	26503.
NextBio	48778.
SOURCE	Search...

Entry information

Entry name

S17A5_HUMAN

Accession

Primary (citable) accession number: Q9NRA2
Secondary accession number(s): Q5SZ76, Q8NBR5, Q9UGH0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	June 7, 2004
Last modified:	May 1, 2013
This is version 95 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.