O75027 (ABCB7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-binding cassette sub-family B member 7, mitochondrial

Alternative name(s):
ATP-binding cassette transporter 7
Short name=ABC transporter 7 protein

Gene names

Name:	ABCB7
Synonyms:	ABC7

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	752 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	Could be involved in the transport of heme from the mitochondria to the cytosol. Plays a central role in the maturation of cytosolic iron-sulfur (Fe/S) cluster-containing proteins.
Subunit structure	Homodimer or heterodimer Potential.
Subcellular location	Mitochondrion inner membrane; Multi-pass membrane protein Potential.
Involvement in disease	Anemia, sideroblastic, spinocerebellar ataxia (ASAT) [MIM:301310]: A X-linked recessive disorder characterized by an infantile to early childhood onset of non-progressive cerebellar ataxia and mild anemia, with hypochromia and microcytosis. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.3 Ref.11 Ref.12
Sequence similarities	Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily. [View classification] Contains 1 ABC transmembrane type-1 domain. Contains 1 ABC transporter domain.

Ontologies

Keywords
Biological process	Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Transit peptide Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular iron ion homeostasis Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	integral to membrane Inferred from Biological aspect of Ancestor. Source: RefGenome mitochondrial inner membrane Inferred from direct assay PubMed 17006453. Source: UniProtKB
Molecular_function	ATP binding Traceable author statement Ref.1. Source: ProtInc ATPase activity, coupled to transmembrane movement of substances Inferred from Biological aspect of Ancestor. Source: RefGenome heme transporter activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: O75027-1)

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: O75027-2)

The sequence of this isoform differs from the canonical sequence as follows:
     56-56: Q → QQ

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 752		ATP-binding cassette sub-family B member 7, mitochondrial		PRO_0000000249
Regions
	Transmembrane	141 – 161	21	Helical; Potential
	Transmembrane	186 – 206	21	Helical; Potential
	Transmembrane	260 – 280	21	Helical; Potential
	Transmembrane	291 – 311	21	Helical; Potential
	Transmembrane	383 – 403	21	Helical; Potential
	Transmembrane	410 – 430	21	Helical; Potential
	Domain	140 – 436	297	ABC transmembrane type-1
	Domain	472 – 706	235	ABC transporter
	Nucleotide binding	505 – 512	8	ATP Potential
Amino acid modifications
	Modified residue	216	1	N6-acetyllysine Ref.9
	Modified residue	251	1	N6-acetyllysine Ref.9
Natural variations
	Alternative sequence	56	1	Q → QQ in isoform 2.		VSP_014635
	Natural variant	208	1	E → D in ASAT. Ref.12		VAR_067354
	Natural variant	315	1	R → G. Ref.1 Ref.11		VAR_022872
	Natural variant	346	1	F → I. Ref.1 Ref.11		VAR_022873
	Natural variant	400	1	I → M in ASAT. Ref.2		VAR_009156
	Natural variant	411	1	V → L in ASAT. Ref.11		VAR_022874
	Natural variant	433	1	E → K in ASAT; impaired maturation of cytosolic Fe/S proteins. Ref.3		VAR_012640
	Natural variant	580	1	A → V. Corresponds to variant rs1340989 [ dbSNP | Ensembl ].		VAR_055471
	Natural variant	581	1	V → A. Corresponds to variant rs1340989 [ dbSNP | Ensembl ].		VAR_037972
Experimental info
	Sequence conflict	141	1	A → P in AAC39865. Ref.4
	Sequence conflict	258	1	R → K in BAA28861. Ref.1
	Sequence conflict	271 – 276	6	LLPIMF → PLPNHV in AAC39865. Ref.4
	Sequence conflict	280	1	L → LL in AAC39865. Ref.4
	Sequence conflict	290	1	G → C in AAC39865. Ref.4
	Sequence conflict	293 – 297	5	FALVT → LLGN in AAC39865. Ref.4
	Sequence conflict	320 – 324	5	IEMNK → LEIDQ in AAC39865. Ref.4
	Sequence conflict	542	1	E → V in AAD47141. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: B1FFA57ABD24FB90	FASTA	752	82,641
	10 20 30 40 50 60 MALLAMHSWR WAAAAAAFEK RRHSAILIRP LVSVSGSGPQ WRPHQLGALG TARAYQIPES 70 80 90 100 110 120 LKSITWQRLG KGNSGQFLDA AKALQVWPLI EKRTCWHGHA GGGLHTDPKE GLKDVDTRKI 130 140 150 160 170 180 IKAMLSYVWP KDRPDLRARV AISLGFLGGA KAMNIVVPFM FKYAVDSLNQ MSGNMLNLSD 190 200 210 220 230 240 APNTVATMAT AVLIGYGVSR AGAAFFNEVR NAVFGKVAQN SIRRIAKNVF LHLHNLDLGF 250 260 270 280 290 300 HLSRQTGALS KAIDRGTRGI SFVLSALVFN LLPIMFEVML VSGVLYYKCG AQFALVTLGT 310 320 330 340 350 360 LGTYTAFTVA VTRWRTRFRI EMNKADNDAG NAAIDSLLNY ETVKYFNNER YEAQRYDGFL 370 380 390 400 410 420 KTYETASLKS TSTLAMLNFG QSAIFSVGLT AIMVLASQGI VAGTLTVGDL VMVNGLLFQL 430 440 450 460 470 480 SLPLNFLGTV YRETRQALID MNTLFTLLKV DTQIKDKVMA SPLQITPQTA TVAFDNVHFE 490 500 510 520 530 540 YIEGQKVLSG ISFEVPAGKK VAIVGGSGSG KSTIVRLLFR FYEPQKGSIY LAGQNIQDVS 550 560 570 580 590 600 LESLRRAVGV VPQDAVLFHN TIYYNLLYGN ISASPEEVYA VAKLAGLHDA ILRMPHGYDT 610 620 630 640 650 660 QVGERGLKLS GGEKQRVAIA RAILKDPPVI LYDEATSSLD SITEETILGA MKDVVKHRTS 670 680 690 700 710 720 IFIAHRLSTV VDADEIIVLD QGKVAERGTH HGLLANPHSI YSEMWHTQSS RVQNHDNPKW 730 740 750 EAKKENISKE EERKKLQEEI VNSVKGCGNC SC
	Isoform 2 [UniParc]. Checksum: 9B96042C55C3C62F	FASTA	753	82,769
	10 20 30 40 50 60 MALLAMHSWR WAAAAAAFEK RRHSAILIRP LVSVSGSGPQ WRPHQLGALG TARAYQQIPE 70 80 90 100 110 120 SLKSITWQRL GKGNSGQFLD AAKALQVWPL IEKRTCWHGH AGGGLHTDPK EGLKDVDTRK 130 140 150 160 170 180 IIKAMLSYVW PKDRPDLRAR VAISLGFLGG AKAMNIVVPF MFKYAVDSLN QMSGNMLNLS 190 200 210 220 230 240 DAPNTVATMA TAVLIGYGVS RAGAAFFNEV RNAVFGKVAQ NSIRRIAKNV FLHLHNLDLG 250 260 270 280 290 300 FHLSRQTGAL SKAIDRGTRG ISFVLSALVF NLLPIMFEVM LVSGVLYYKC GAQFALVTLG 310 320 330 340 350 360 TLGTYTAFTV AVTRWRTRFR IEMNKADNDA GNAAIDSLLN YETVKYFNNE RYEAQRYDGF 370 380 390 400 410 420 LKTYETASLK STSTLAMLNF GQSAIFSVGL TAIMVLASQG IVAGTLTVGD LVMVNGLLFQ 430 440 450 460 470 480 LSLPLNFLGT VYRETRQALI DMNTLFTLLK VDTQIKDKVM ASPLQITPQT ATVAFDNVHF 490 500 510 520 530 540 EYIEGQKVLS GISFEVPAGK KVAIVGGSGS GKSTIVRLLF RFYEPQKGSI YLAGQNIQDV 550 560 570 580 590 600 SLESLRRAVG VVPQDAVLFH NTIYYNLLYG NISASPEEVY AVAKLAGLHD AILRMPHGYD 610 620 630 640 650 660 TQVGERGLKL SGGEKQRVAI ARAILKDPPV ILYDEATSSL DSITEETILG AMKDVVKHRT 670 680 690 700 710 720 SIFIAHRLST VVDADEIIVL DQGKVAERGT HHGLLANPHS IYSEMWHTQS SRVQNHDNPK 730 740 750 WEAKKENISK EEERKKLQEE IVNSVKGCGN CSC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and chromosomal mapping of a novel ABC transporter gene (hABC7), a candidate for X-linked sideroblastic anemia with spinocerebellar ataxia." Shimada Y., Okuno S., Kawai A., Shinomiya H., Saito A., Suzuki M., Omori Y., Nishino N., Kanemoto N., Fujiwara T., Horie M., Takahashi E. J. Hum. Genet. 43:115-122(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLY-315 AND ILE-346. Tissue: Placenta.
[2]	"Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-linked sideroblastic anemia and ataxia (XLSA/A)." Allikmets R., Raskind W.H., Hutchinson A., Schueck N.D., Dean M., Koeller D.M. Hum. Mol. Genet. 8:743-749(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASAT MET-400.
[3]	"Human ABC7 transporter: gene structure and mutation causing X-linked sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur protein maturation." Bekri S., Kispal G., Lange H., Fitzsimons E., Tolmie J., Lill R., Bishop D.F. Blood 96:3256-3264(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASAT LYS-433.
[4]	"Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning." Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z. Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Umbilical cord blood.
[5]	"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 (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: Muscle.
[8]	"Identification of a human mitochondrial ABC transporter, the functional orthologue of yeast Atm1p." Csere P., Lill R., Kispal G. FEBS Lett. 441:266-270(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-752 (ISOFORM 1).
[9]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-216 AND LYS-251, MASS SPECTROMETRY.
[10]	"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].
[11]	"X-linked cerebellar ataxia and sideroblastic anaemia associated with a missense mutation in the ABC7 gene predicting V411L." Maguire A., Hellier K., Hammans S., May A. Br. J. Haematol. 115:910-917(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ASAT LEU-411, VARIANTS GLY-315 AND ILE-346.
[12]	"X-linked sideroblastic anemia and ataxia: A new family with identification of a fourth ABCB7 gene mutation." D'Hooghe M., Selleslag D., Mortier G., Van Coster R., Vermeersch P., Billiet J., Bekri S. Eur. J. Paediatr. Neurol. 16:730-735(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ASAT ASP-208.
+	Additional computationally mapped references.

Web resources

GeneReviews

ABCMdb

Database for mutations in ABC proteins

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB005289 mRNA. Translation: BAA28861.1. AF133659 mRNA. Translation: AAD33045.1. AF241887 , AF241872, AF241873, AF241874, AF241875, AF241876, AF241877, AF241878, AF241879, AF241880, AF241881, AF241882, AF241883, AF241884, AF241885, AF241886 Genomic DNA. Translation: AAK20173.1. AF038950 mRNA. Translation: AAC39865.1. BT009918 mRNA. Translation: AAP88920.1. AL360179, AL359545 Genomic DNA. Translation: CAH70564.1. AL360179, AL359545 Genomic DNA. Translation: CAH70565.1. AL359545, AL360179 Genomic DNA. Translation: CAI41573.1. AL359545, AL360179 Genomic DNA. Translation: CAI41574.1. BC006323 mRNA. Translation: AAH06323.1. AF078777 mRNA. Translation: AAD47141.1.
IPI	IPI00306748. IPI00556553.
RefSeq	NP_001258625.1. NM_001271696.1. NP_001258627.1. NM_001271698.1. NP_004290.2. NM_004299.4.
UniGene	Hs.370480.
3D structure databases
ProteinModelPortal	O75027.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75027. 1 interaction.
STRING	9606.ENSP00000253577.
Protein family/group databases
TCDB	3.A.1.210.4. ATP-binding cassette (ABC) superfamily.
PTM databases
PhosphoSite	O75027.
Proteomic databases
PaxDb	O75027.
PRIDE	O75027.
Protocols and materials databases
DNASU	22.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000253577; ENSP00000253577; ENSG00000131269. ENST00000373394; ENSP00000362492; ENSG00000131269.
GeneID	22.
KEGG	hsa:22.
UCSC	uc004ebz.3. human. uc004eca.3. human.
Organism-specific databases
CTD	22.
GeneCards	GC0XM074189.
H-InvDB	HIX0028475.
HGNC	HGNC:48. ABCB7.
HPA	HPA034982.
MIM	300135. gene. 301310. phenotype.
neXtProt	NX_O75027.
Orphanet	2802. X-linked sideroblastic anemia - ataxia.
PharmGKB	PA24389.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5265.
HOVERGEN	HBG080194.
KO	K05662.
OMA	RYEAQRY.
Enzyme and pathway databases
Reactome	REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	O75027.
Bgee	O75027.
CleanEx	HS_ABCB7.
Genevestigator	O75027.
GermOnline	ENSG00000131269. Homo sapiens.
Family and domain databases
InterPro	IPR003593. AAA+_ATPase. IPR003439. ABC_transporter-like. IPR017871. ABC_transporter_CS. IPR017940. ABC_transporter_type1. IPR001140. ABC_transptr_TM_dom. IPR011527. ABC_transptrTM_dom_typ1. [Graphical view]
Pfam	PF00664. ABC_membrane. 1 hit. PF00005. ABC_tran. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
SUPFAM	SSF90123. ABC_TM_1. 1 hit.
PROSITE	PS50929. ABC_TM1F. 1 hit. PS00211. ABC_TRANSPORTER_1. 1 hit. PS50893. ABC_TRANSPORTER_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	22.
NextBio	65.
SOURCE	Search...

Entry information

Entry name

ABCB7_HUMAN

Accession

Primary (citable) accession number: O75027
Secondary accession number(s): O75345 , Q5VWY7, Q5VWY8, Q9BRE1, Q9UND1, Q9UP01

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 128 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.