Q9H0F7 (ARL6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ADP-ribosylation factor-like protein 6

Alternative name(s):
Bardet-Biedl syndrome 3 protein

Gene names

Name:

ARL6

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

General annotation (Comments)

Function	Involved in membrane protein trafficking at the base of the ciliary organelle. Mediates recruitment onto plasma membrane of the BBSome complex which would constitute a coat complex required for sorting of specific membrane proteins to the primary cilia. May regulate cilia assembly and disassembly and subsequent ciliary signaling events such as the Wnt signaling cascade. Isoform 2 may be required for proper retinal function and organization. Ref.7 Ref.10
Subunit structure	Interacts with SEC61B, ARL6IP1, ARL6IP2, ARL6IP3, ARL6IP4 ARL6IP5 and ARL6IP6 By similarity. Interacts (GTP-bound form) with the BBSome a complex that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8, BBS9 and BBIP10. Ref.7
Subcellular location	Cell projection › cilium membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › cytoskeleton › cilium axoneme. Cytoplasm › cytoskeleton › cilium basal body. Note: Appears in a pattern of punctae flanking the microtubule axoneme that likely correspond to small membrane-associated patches. Localizes to the so-called ciliary gate where vesicles carrying ciliary cargo fuse with the membrane. Ref.7 Ref.10
Involvement in disease	Bardet-Biedl syndrome 3 (BBS3) [MIM:209900]: A syndrome characterized by usually severe pigmentary retinopathy, early-onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.11 Retinitis pigmentosa 55 (RP55) [MIM:613575]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13
Sequence similarities	Belongs to the small GTPase superfamily. Arf family.

Ontologies

Keywords
Biological process	Cilium biogenesis/degradation Sensory transduction Vision
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Disease	Bardet-Biedl syndrome Ciliopathy Disease mutation Mental retardation Obesity Retinitis pigmentosa
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
PTM	Lipoprotein Myristate
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway Inferred from mutant phenotype Ref.10. Source: UniProtKB cilium assembly Inferred from mutant phenotype Ref.10. Source: UniProtKB determination of left/right symmetry Inferred from sequence or structural similarity. Source: BHF-UCL fat cell differentiation Inferred from electronic annotation. Source: Compara melanosome transport Inferred from sequence or structural similarity. Source: BHF-UCL protein polymerization Inferred from sequence or structural similarity. Source: UniProtKB protein targeting to membrane Inferred from sequence or structural similarity. Source: UniProtKB small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	axonemal microtubule Inferred from sequence or structural similarity. Source: UniProtKB cilium axoneme Inferred from sequence or structural similarity. Source: UniProtKB cilium membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane coat Inferred from sequence or structural similarity. Source: UniProtKB microtubule basal body Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipid binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BBS1	Q8NFJ9	4	EBI-2891949,EBI-1805484

Alternative products

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

Isoform 1 (identifier: Q9H0F7-1)

Also known as: BBS3;

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: Q9H0F7-2)

Also known as: BBS3L;

The sequence of this isoform differs from the canonical sequence as follows:
     179-186: DQIQTVKT → EKTIQSDPDCEDMKR

Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 186

186

ADP-ribosylation factor-like protein 6

PRO_0000207472

Regions

Nucleotide binding

24 – 31

8

GTP

Nucleotide binding

69 – 73

5

GTP By similarity

Nucleotide binding

130 – 133

4

GTP

Sites

Metal binding

31

1

Magnesium

Metal binding

50

1

Magnesium

Binding site

50

1

GTP

Binding site

72

1

GTP; via amide nitrogen

Binding site

164

1

GTP; via amide nitrogen

Amino acid modifications

Lipidation

2

1

N-myristoyl glycine Potential

Natural variations

Alternative sequence

179 – 186

8

DQIQTVKT → EKTIQSDPDCEDMKR in isoform 2.

VSP_040511

Natural variant

31

1

T → M in BBS3; abrogates the GTP-binding ability without affecting GDP-binding/dissociating properties; increased proteasomal degradation. Ref.10 Ref.11 Ref.12

VAR_027643

Natural variant

31

1

T → R in BBS3; locked in a GDP-bound state that differs from its wild-type counterpart which is mainly GTP-bound; increased proteasomal degradation. Ref.10 Ref.11 Ref.12

VAR_027644

Natural variant

89

1

A → V in RP55. Ref.13

VAR_064184

Natural variant

169

1

G → A in BBS3; abrogates the GTP-binding ability; increased proteasomal degradation. Ref.10 Ref.11 Ref.12

VAR_027645

Natural variant

170

1

L → W in BBS3; abrogates the GTP-binding ability; increased proteasomal degradation. Ref.10 Ref.11 Ref.12

VAR_027646

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

186

Helix Strand Turn

Details...

Beta strand

18 – 24

7

Helix

30 – 36

7

Helix

40 – 42

3

Beta strand

51 – 59

9

Beta strand

64 – 70

7

Turn

74 – 76

3

Helix

77 – 86

10

Beta strand

88 – 95

8

Helix

99 – 114

16

Turn

116 – 120

5

Beta strand

125 – 130

6

Helix

140 – 147

8

Helix

149 – 151

3

Beta strand

157 – 161

5

Turn

164 – 167

4

Helix

170 – 180

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (BBS3) [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 42E37FC7886BF1F0	FASTA	186	21,097
	10 20 30 40 50 60 MGLLDRLSVL LGLKKKEVHV LCLGLDNSGK TTIINKLKPS NAQSQNILPT IGFSIEKFKS 70 80 90 100 110 120 SSLSFTVFDM SGQGRYRNLW EHYYKEGQAI IFVIDSSDRL RMVVAKEELD TLLNHPDIKH 130 140 150 160 170 180 RRIPILFFAN KMDLRDAVTS VKVSQLLCLE NIKDKPWHIC ASDAIKGEGL QEGVDWLQDQ IQTVKT
	Isoform 2 (BBS3L) [UniParc]. Checksum: 4C6C43101CE360C1	FASTA	193	21,960
	10 20 30 40 50 60 MGLLDRLSVL LGLKKKEVHV LCLGLDNSGK TTIINKLKPS NAQSQNILPT IGFSIEKFKS 70 80 90 100 110 120 SSLSFTVFDM SGQGRYRNLW EHYYKEGQAI IFVIDSSDRL RMVVAKEELD TLLNHPDIKH 130 140 150 160 170 180 RRIPILFFAN KMDLRDAVTS VKVSQLLCLE NIKDKPWHIC ASDAIKGEGL QEGVDWLQEK 190 TIQSDPDCED MKR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[2]	"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]. Tissue: Trachea.
[3]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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].
[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]. Tissue: Testis.
[6]	"Comparative genomic analysis identifies an ADP-ribosylation factor-like gene as the cause of Bardet-Biedl Syndrome (BBS3)." Chiang A.P., Nishimura D., Searby C., Elbedour K., Carmi R., Ferguson A.L., Secrist J., Braun T., Casavant T., Stone E.M., Sheffield V.C. Am. J. Hum. Genet. 75:475-484(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN BBS3.
[7]	"The conserved Bardet-Biedl syndrome proteins assemble a coat that traffics membrane proteins to cilia." Jin H., White S.R., Shida T., Schulz S., Aguiar M., Gygi S.P., Bazan J.F., Nachury M.V. Cell 141:1208-1219(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE BBSOME.
[8]	"Identification and functional analysis of the vision-specific BBS3 (ARL6) long isoform." Pretorius P.R., Baye L.M., Nishimura D.Y., Searby C.C., Bugge K., Yang B., Mullins R.F., Stone E.M., Sheffield V.C., Slusarski D.C. PLoS Genet. 6:E1000884-E1000884(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORM 2).
[9]	"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].
[10]	"Bardet-Biedl syndrome-associated small GTPase ARL6 (BBS3) functions at or near the ciliary gate and modulates Wnt signaling." Wiens C.J., Tong Y., Esmail M.A., Oh E., Gerdes J.M., Wang J., Tempel W., Rattner J.B., Katsanis N., Park H.W., Leroux M.R. J. Biol. Chem. 285:16218-16230(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 16-186 IN COMPLEX WITH GTP AND MAGNESIUM, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS MET-31; ARG-31; ALA-169 AND TRP-170.
[11]	"Mutations in a member of the Ras superfamily of small GTP-binding proteins causes Bardet-Biedl syndrome." Fan Y., Esmail M.A., Ansley S.J., Blacque O.E., Boroevich K., Ross A.J., Moore S.J., Badano J.L., May-Simera H., Compton D.S., Green J.S., Lewis R.A., van Haelst M.M., Parfrey P.S., Baillie D.L., Beales P.L., Katsanis N., Davidson W.S., Leroux M.R. Nat. Genet. 36:989-993(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS BBS3 ARG-31; MET-31; ALA-169 AND TRP-170.
[12]	"Biochemical characterization of missense mutations in the Arf/Arl-family small GTPase Arl6 causing Bardet-Biedl syndrome." Kobayashi T., Hori Y., Ueda N., Kajiho H., Muraoka S., Shima F., Kataoka T., Kontani K., Katada T. Biochem. Biophys. Res. Commun. 381:439-442(2009) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS MET-31; ARG-31; ALA-169 AND TRP-170.
[13]	"Molecular characterization of retinitis pigmentosa in Saudi Arabia." Aldahmesh M.A., Safieh L.A., Alkuraya H., Al-Rajhi A., Shamseldin H., Hashem M., Alzahrani F., Khan A.O., Alqahtani F., Rahbeeni Z., Alowain M., Khalak H., Al-Hazzaa S., Meyer B.F., Alkuraya F.S. Mol. Vis. 15:2464-2469(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP55 VAL-89.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL136815 mRNA. Translation: CAB66749.1.
AK292958 mRNA. Translation: BAF85647.1.
AC110491 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79880.1.
CH471052 Genomic DNA. Translation: EAW79881.1.
CH471052 Genomic DNA. Translation: EAW79882.1.
CH471052 Genomic DNA. Translation: EAW79883.1.
CH471052 Genomic DNA. Translation: EAW79884.1.
BC024239 mRNA. Translation: AAH24239.1.

IPI

IPI00021685.
IPI00974545.

RefSeq

NP_115522.1. NM_032146.3.
NP_816931.1. NM_177976.1.

UniGene

Hs.373801.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2H57	X-ray	2.00	A/B/C	16-186	[»]

ProteinModelPortal

Q9H0F7.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H0F7. 15 interactions.

STRING

9606.ENSP00000337722.

PTM databases

PhosphoSite

Q9H0F7.

Polymorphism databases

DMDM

14547903.

Proteomic databases

PaxDb

Q9H0F7.

PRIDE

Q9H0F7.

Protocols and materials databases

DNASU

84100.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000335979; ENSP00000337722; ENSG00000113966.
ENST00000394206; ENSP00000377756; ENSG00000113966.
ENST00000463745; ENSP00000419619; ENSG00000113966.
ENST00000493990; ENSP00000418057; ENSG00000113966.

GeneID

84100.

KEGG

hsa:84100.

UCSC

uc003dru.3. human.

Organism-specific databases

CTD

84100.

GeneCards

GC03P097483.

HGNC

HGNC:13210. ARL6.

HPA

HPA019361.

MIM

209900. phenotype.
608845. gene.
613575. phenotype.

neXtProt

NX_Q9H0F7.

Orphanet

110. Bardet-Biedl syndrome.
791. Retinitis pigmentosa.

PharmGKB

PA134931939.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOGENOM

HOG000163691.

HOVERGEN

HBG002073.

InParanoid

Q9H0F7.

KO

K07951.

OMA

VAKDELD.

OrthoDB

EOG451DRV.

PhylomeDB

Q9H0F7.

Gene expression databases

ArrayExpress

Q9H0F7.

Bgee

Q9H0F7.

CleanEx

HS_ARL6.

Genevestigator

Q9H0F7.

GermOnline

ENSG00000113966. Homo sapiens.

Family and domain databases

InterPro

IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
[Graphical view]

Pfam

PF00025. Arf. 1 hit.
[Graphical view]

PRINTS

PR00328. SAR1GTPBP.

SMART

SM00177. ARF. 1 hit.
[Graphical view]

SUPFAM

SSF52540. SSF52540. 1 hit.

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51417. ARF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ARL6. human.

EvolutionaryTrace

Q9H0F7.

GenomeRNAi

84100.

NextBio

73343.

SOURCE

Search...

Entry information

Entry name

ARL6_HUMAN

Accession

Primary (citable) accession number: Q9H0F7
Secondary accession number(s): A8KA93, D3DN31

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	March 1, 2001
Last modified:	May 29, 2013
This is version 115 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.