O60313 (OPA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dynamin-like 120 kDa protein, mitochondrial
EC=3.6.5.5

Alternative name(s):
Optic atrophy protein 1

Cleaved into the following chain:

1. Dynamin-like 120 kDa protein, form S1

Gene names

Name:	OPA1
Synonyms:	KIAA0567

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	960 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	Dynamin-related GTPase required for mitochondrial fusion and regulation of apoptosis. May form a diffusion barrier for proteins stored in mitochondrial cristae. Proteolytic processing in response to intrinsic apoptotic signals may lead to disassembly of OPA1 oligomers and release of the caspase activator cytochrome C (CYCS) into the mitochondrial intermembrane space. Ref.10 Ref.11 Dynamin-like 120 kDa protein, form S1: Inactive form produced by cleavage at S1 position by OMA1 following stress conditions that induce loss of mitochondrial membrane potential, leading to negative regulation of mitochondrial fusion. Ref.10 Ref.11
Catalytic activity	GTP + H2O = GDP + phosphate.
Subunit structure	Oligomeric complex consisting of membrane-bound and soluble forms of OPA1. Interacts with CHCHD3 and IMMT; these interactions occur preferentially with soluble OPA1 forms. Binds PARL By similarity. Ref.14
Subcellular location	Mitochondrion inner membrane; Single-pass membrane protein. Mitochondrion intermembrane space Ref.7 Ref.10.
Tissue specificity	Highly expressed in retina. Also expressed in brain, testis, heart and skeletal muscle. Isoform 1 expressed in retina, skeletal muscle, heart, lung, ovary, colon, thyroid gland, leukocytes and fetal brain. Isoform 2 expressed in colon, liver, kidney, thyroid gland and leukocytes. Low levels of all isoforms expressed in a variety of tissues. Ref.6 Ref.7 Ref.8
Post-translational modification	PARL-dependent proteolytic processing releases an antiapoptotic soluble form not required for mitochondrial fusion. Cleaved by OMA1 at position S1 following stress conditions.
Involvement in disease	Optic atrophy 1 (OPA1) [MIM:165500]: A condition that features progressive visual loss in association with optic atrophy. Atrophy of the optic disk indicates a deficiency in the number of nerve fibers which arise in the retina and converge to form the optic disk, optic nerve, optic chiasm and optic tracts. OPA1 is characterized by an insidious onset of visual impairment in early childhood with moderate to severe loss of visual acuity, temporal optic disk pallor, color vision deficits, and centrocecal scotoma of variable density. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.7 Ref.8 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.23 Ref.24 Ref.26 Ref.27 Ref.28 Dominant optic atrophy plus syndrome (DOA+) [MIM:125250]: A neurologic disorder characterized most commonly by an insidious onset of visual loss and sensorineural hearing loss in childhood with variable presentation of other clinical manifestations including progressive external ophthalmoplegia, muscle cramps, hyperreflexia, and ataxia. There appears to be a wide range of intermediate phenotypes. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.22 Ref.25
Sequence similarities	Belongs to the dynamin family.
Sequence caution	The sequence AF416919 differs from that shown. Reason:

Ontologies

Keywords
Biological process	Apoptosis Sensory transduction Vision
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Deafness Disease mutation
Domain	Coiled coil Transit peptide Transmembrane Transmembrane helix
Ligand	GTP-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW axon transport of mitochondrion Traceable author statement Ref.8. Source: UniProtKB cellular senescence Inferred from direct assay PubMed 17545159. Source: UniProtKB inner mitochondrial membrane organization Inferred from direct assay PubMed 12509422. Source: UniProtKB mitochondrial fission Traceable author statement PubMed 12509422. Source: UniProtKB mitochondrial fusion Inferred from direct assay PubMed 17545159. Source: UniProtKB negative regulation of release of cytochrome c from mitochondria Inferred from mutant phenotype PubMed 21149567. Source: UniProtKB neural tube closure Inferred from electronic annotation. Source: Compara visual perception Inferred from mutant phenotype Ref.8. Source: UniProtKB
Cellular_component	dendrite Inferred from sequence or structural similarity PubMed 11847212. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial crista Inferred from direct assay PubMed 12504110. Source: UniProtKB mitochondrial intermembrane space Inferred from sequence or structural similarity PubMed 11847212. Source: UniProtKB mitochondrial outer membrane Inferred from direct assay PubMed 12504110. Source: UniProtKB
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Traceable author statement Ref.8. Source: UniProtKB magnesium ion binding Non-traceable author statement Ref.8. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BNIP3	Q12983	10	EBI-1054131,EBI-749464

Alternative products

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

Isoform 1 (identifier: O60313-1)

Also known as: 6;

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: O60313-2)

The sequence of this isoform differs from the canonical sequence as follows:
     209-209: V → GLLGELILLQQQIQEHEEEARRAAGQYSTSYAQQKRKV

Note: Proteolytic processing near Gln-220 produces form S2.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 87	87	Mitochondrion By similarity
	Chain	88 – 960	873	Dynamin-like 120 kDa protein, mitochondrial		PRO_0000007397
	Chain	195 – 960	766	Dynamin-like 120 kDa protein, form S1 By similarity		PRO_0000253479
Regions
	Topological domain	88 – 96	9	Mitochondrial matrix By similarity
	Transmembrane	97 – 113	17	Helical; Potential
	Topological domain	114 – 960	847	Mitochondrial intermembrane By similarity
	Nucleotide binding	295 – 302	8	GTP Potential
	Nucleotide binding	398 – 402	5	GTP Potential
	Nucleotide binding	467 – 470	4	GTP Potential
	Coiled coil	210 – 254	45	Potential
	Coiled coil	895 – 960	66	Potential
Amino acid modifications
	Modified residue	228	1	N6-acetyllysine Ref.12
	Modified residue	652	1	Phosphothreonine By similarity
	Modified residue	929	1	Phosphothreonine Ref.9
Natural variations
	Alternative sequence	209	1	V → GLLGELILLQQQIQEHEEEA RRAAGQYSTSYAQQKRKV in isoform 2.		VSP_021035
	Natural variant	8	1	A → S in OPA1. Ref.23		VAR_060825
	Natural variant	38 – 43	6	Missing in OPA1.		VAR_022923
	Natural variant	80	1	Y → C in OPA1. Ref.23		VAR_060826
	Natural variant	95	1	T → M in OPA1. Ref.26		VAR_060827
	Natural variant	102	1	Y → C in OPA1. Ref.26		VAR_060828
	Natural variant	158	1	S → N. Ref.1 Ref.5 Ref.15 Ref.16 Ref.17 Ref.21 Ref.23 Corresponds to variant rs7624750 [ dbSNP | Ensembl ].		VAR_022924
	Natural variant	167	1	P → L. Ref.17		VAR_022925
	Natural variant	192	1	A → V. Ref.15 Ref.17 Ref.23 Corresponds to variant rs34307082 [ dbSNP | Ensembl ].		VAR_022926
	Natural variant	270	1	E → K in OPA1. Ref.15		VAR_060829
	Natural variant	272	1	L → P in OPA1. Ref.19		VAR_060830
	Natural variant	273	1	D → A in OPA1. Ref.15		VAR_060831
	Natural variant	290	1	R → Q in OPA1. Ref.6 Ref.8 Ref.15 Ref.16		VAR_011483
	Natural variant	290	1	R → W in OPA1. Ref.15		VAR_060832
	Natural variant	293 – 294	2	Missing in OPA1.		VAR_060833
	Natural variant	300	1	G → E in OPA1. Ref.7 Ref.16		VAR_011484
	Natural variant	310	1	Q → R in OPA1. Ref.26		VAR_060834
	Natural variant	324 – 326	3	Missing in OPA1.		VAR_060835
	Natural variant	357	1	A → T in OPA1. Ref.26		VAR_060836
	Natural variant	382	1	I → M in OPA1. Ref.26		VAR_060837
	Natural variant	384	1	L → F in OPA1. Ref.16		VAR_060838
	Natural variant	396	1	L → P in OPA1. Ref.26		VAR_060839
	Natural variant	396	1	L → R in OPA1. Ref.17		VAR_022927
	Natural variant	400	1	P → A in OPA1. Ref.28		VAR_067355
	Natural variant	429 – 430	2	Missing in OPA1.		VAR_060840
	Natural variant	430	1	N → D in OPA1. Ref.26		VAR_060841
	Natural variant	432	1	Missing in OPA1. Ref.8 Ref.17		VAR_011485
	Natural variant	438	1	D → V in OPA1. Ref.15		VAR_060842
	Natural variant	445	1	R → H in OPA1 and DOA+. Ref.18 Ref.20 Ref.22		VAR_015741
	Natural variant	449	1	T → R in OPA1. Ref.26		VAR_060843
	Natural variant	463	1	I → IFIF in OPA1.		VAR_060844
	Natural variant	468	1	K → E in OPA1. Ref.15		VAR_060845
	Natural variant	470	1	D → G in OPA1. Ref.19		VAR_060846
	Natural variant	487	1	E → K in OPA1. Ref.26		VAR_060847
	Natural variant	503	1	T → K in OPA1. Ref.16 Ref.17		VAR_022928
	Natural variant	505	1	K → N in OPA1. Ref.16		VAR_060848
	Natural variant	545	1	S → R in OPA1. Ref.24 Ref.26		VAR_026533
	Natural variant	550	1	D → N. Ref.15		VAR_060849
	Natural variant	551	1	C → Y in OPA1. Ref.26		VAR_060851
	Natural variant	551	1	Missing in OPA1. Ref.15		VAR_060850
	Natural variant	571	1	R → H in OPA1. Ref.17		VAR_022929
	Natural variant	574	1	L → P in OPA1. Ref.19		VAR_060852
	Natural variant	582	1	Y → C in DOA+. Ref.25		VAR_060853
	Natural variant	586 – 589	4	Missing in OPA1.		VAR_022930
	Natural variant	590	1	R → Q in OPA1. Ref.26		VAR_060854
	Natural variant	590	1	R → W in OPA1. Ref.21		VAR_060855
	Natural variant	593	1	L → P in OPA1. Ref.26		VAR_060856
	Natural variant	646	1	S → L in OPA1. Ref.26		VAR_060857
	Natural variant	700 – 701	2	Missing in OPA1.		VAR_060858
	Natural variant	728	1	N → K in OPA1. Ref.21		VAR_060859
	Natural variant	768	1	G → D in OPA1. Ref.26		VAR_060860
	Natural variant	781	1	R → W in OPA1. Ref.26		VAR_060861
	Natural variant	785	1	Q → R in OPA1. Ref.6 Ref.15		VAR_060862
	Natural variant	823	1	S → Y in OPA1. Ref.26		VAR_060863
	Natural variant	841	1	Y → C in OPA1. Ref.23		VAR_060864
	Natural variant	882	1	R → L in OPA1. Ref.26		VAR_060865
	Natural variant	887	1	L → P in OPA1. Ref.26		VAR_060866
	Natural variant	907	1	E → G. Ref.16		VAR_060867
	Natural variant	932	1	R → C in OPA1. Ref.26 Ref.27		VAR_060868
	Natural variant	939	1	L → P in OPA1. Ref.6		VAR_028370
	Natural variant	949	1	L → P in OPA1. Ref.26		VAR_060869

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (6) [UniParc]. Last modified November 25, 2008. Version 3. Checksum: 1C397109787AEB4D	FASTA	960	111,631
	10 20 30 40 50 60 MWRLRRAAVA CEVCQSLVKH SSGIKGSLPL QKLHLVSRSI YHSHHPTLKL QRPQLRTSFQ 70 80 90 100 110 120 QFSSLTNLPL RKLKFSPIKY GYQPRRNFWP ARLATRLLKL RYLILGSAVG GGYTAKKTFD 130 140 150 160 170 180 QWKDMIPDLS EYKWIVPDIV WEIDEYIDFE KIRKALPSSE DLVKLAPDFD KIVESLSLLK 190 200 210 220 230 240 DFFTSGSPEE TAFRATDRGS ESDKHFRKVS DKEKIDQLQE ELLHTQLKYQ RILERLEKEN 250 260 270 280 290 300 KELRKLVLQK DDKGIHHRKL KKSLIDMYSE VLDVLSDYDA SYNTQDHLPR VVVVGDQSAG 310 320 330 340 350 360 KTSVLEMIAQ ARIFPRGSGE MMTRSPVKVT LSEGPHHVAL FKDSSREFDL TKEEDLAALR 370 380 390 400 410 420 HEIELRMRKN VKEGCTVSPE TISLNVKGPG LQRMVLVDLP GVINTVTSGM APDTKETIFS 430 440 450 460 470 480 ISKAYMQNPN AIILCIQDGS VDAERSIVTD LVSQMDPHGR RTIFVLTKVD LAEKNVASPS 490 500 510 520 530 540 RIQQIIEGKL FPMKALGYFA VVTGKGNSSE SIEAIREYEE EFFQNSKLLK TSMLKAHQVT 550 560 570 580 590 600 TRNLSLAVSD CFWKMVRESV EQQADSFKAT RFNLETEWKN NYPRLRELDR NELFEKAKNE 610 620 630 640 650 660 ILDEVISLSQ VTPKHWEEIL QQSLWERVST HVIENIYLPA AQTMNSGTFN TTVDIKLKQW 670 680 690 700 710 720 TDKQLPNKAV EVAWETLQEE FSRFMTEPKG KEHDDIFDKL KEAVKEESIK RHKWNDFAED 730 740 750 760 770 780 SLRVIQHNAL EDRSISDKQQ WDAAIYFMEE ALQARLKDTE NAIENMVGPD WKKRWLYWKN 790 800 810 820 830 840 RTQEQCVHNE TKNELEKMLK CNEEHPAYLA SDEITTVRKN LESRGVEVDP SLIKDTWHQV 850 860 870 880 890 900 YRRHFLKTAL NHCNLCRRGF YYYQRHFVDS ELECNDVVLF WRIQRMLAIT ANTLRQQLTN 910 920 930 940 950 960 TEVRRLEKNV KEVLEDFAED GEKKIKLLTG KRVQLAEDLK KVREIQEKLD AFIEALHQEK
	Isoform 2 [UniParc]. Checksum: 5D1F6B9BF800F35E	FASTA	997	115,884
	10 20 30 40 50 60 MWRLRRAAVA CEVCQSLVKH SSGIKGSLPL QKLHLVSRSI YHSHHPTLKL QRPQLRTSFQ 70 80 90 100 110 120 QFSSLTNLPL RKLKFSPIKY GYQPRRNFWP ARLATRLLKL RYLILGSAVG GGYTAKKTFD 130 140 150 160 170 180 QWKDMIPDLS EYKWIVPDIV WEIDEYIDFE KIRKALPSSE DLVKLAPDFD KIVESLSLLK 190 200 210 220 230 240 DFFTSGSPEE TAFRATDRGS ESDKHFRKGL LGELILLQQQ IQEHEEEARR AAGQYSTSYA 250 260 270 280 290 300 QQKRKVSDKE KIDQLQEELL HTQLKYQRIL ERLEKENKEL RKLVLQKDDK GIHHRKLKKS 310 320 330 340 350 360 LIDMYSEVLD VLSDYDASYN TQDHLPRVVV VGDQSAGKTS VLEMIAQARI FPRGSGEMMT 370 380 390 400 410 420 RSPVKVTLSE GPHHVALFKD SSREFDLTKE EDLAALRHEI ELRMRKNVKE GCTVSPETIS 430 440 450 460 470 480 LNVKGPGLQR MVLVDLPGVI NTVTSGMAPD TKETIFSISK AYMQNPNAII LCIQDGSVDA 490 500 510 520 530 540 ERSIVTDLVS QMDPHGRRTI FVLTKVDLAE KNVASPSRIQ QIIEGKLFPM KALGYFAVVT 550 560 570 580 590 600 GKGNSSESIE AIREYEEEFF QNSKLLKTSM LKAHQVTTRN LSLAVSDCFW KMVRESVEQQ 610 620 630 640 650 660 ADSFKATRFN LETEWKNNYP RLRELDRNEL FEKAKNEILD EVISLSQVTP KHWEEILQQS 670 680 690 700 710 720 LWERVSTHVI ENIYLPAAQT MNSGTFNTTV DIKLKQWTDK QLPNKAVEVA WETLQEEFSR 730 740 750 760 770 780 FMTEPKGKEH DDIFDKLKEA VKEESIKRHK WNDFAEDSLR VIQHNALEDR SISDKQQWDA 790 800 810 820 830 840 AIYFMEEALQ ARLKDTENAI ENMVGPDWKK RWLYWKNRTQ EQCVHNETKN ELEKMLKCNE 850 860 870 880 890 900 EHPAYLASDE ITTVRKNLES RGVEVDPSLI KDTWHQVYRR HFLKTALNHC NLCRRGFYYY 910 920 930 940 950 960 QRHFVDSELE CNDVVLFWRI QRMLAITANT LRQQLTNTEV RRLEKNVKEV LEDFAEDGEK 970 980 990 KIKLLTGKRV QLAEDLKKVR EIQEKLDAFI EALHQEK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASN-158. Tissue: Brain.
[2]	"Identification of rare DNA variants in mitochondrial disorders with improved array-based sequencing." Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R., Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W., Mindrinos M., Speed T.P., Scharfe C. Nucleic Acids Res. 39:44-58(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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] (ISOFORM 1), VARIANT ASN-158. Tissue: Brain.
[6]	"Mutation spectrum and splicing variants in the OPA1 gene." Delettre C., Griffoin J.-M., Kaplan J., Dollfus H., Lorenz B., Faivre L., Lenaers G., Belenguer P., Hamel C.P. Hum. Genet. 109:584-591(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2), TISSUE SPECIFICITY, VARIANTS OPA1 GLN-290; ARG-785 AND PRO-939.
[7]	"Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy." Delettre C., Lenaers G., Griffoin J.-M., Gigarel N., Lorenzo C., Belenguer P., Pelloquin L., Grosgeorge J., Turc-Carel C., Perret E., Astarie-Dequeker C., Lasquellec L., Arnaud B., Ducommun B., Kaplan J., Hamel C.P. Nat. Genet. 26:207-210(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT OPA1 GLU-300.
[8]	"OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28." Alexander C., Votruba M., Pesch U.E.A., Thiselton D.L., Mayer S., Moore A., Rodriguez M., Kellner U., Leo-Kottler B., Auburger G., Bhattacharya S.S., Wissinger B. Nat. Genet. 26:211-215(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, VARIANTS OPA1 GLN-290 AND ILE-432 DEL.
[9]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-929, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"Regulation of mitochondrial morphology through proteolytic cleavage of OPA1." Ishihara N., Fujita Y., Oka T., Mihara K. EMBO J. 25:2966-2977(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]	"Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells." Head B., Griparic L., Amiri M., Gandre-Babbe S., van der Bliek A.M. J. Cell Biol. 187:959-966(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION (DYNAMIN-LIKE 120 KDA PROTEIN; FORM S1), PROTEOLYTIC PROCESSING.
[12]	"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-228, MASS SPECTROMETRY.
[13]	"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].
[14]	"ChChd3, an inner mitochondrial membrane protein, is essential for maintaining crista integrity and mitochondrial function." Darshi M., Mendiola V.L., Mackey M.R., Murphy A.N., Koller A., Perkins G.A., Ellisman M.H., Taylor S.S. J. Biol. Chem. 286:2918-2932(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CHCHD3 AND IMMT.
[15]	"OPA1 mutations in patients with autosomal dominant optic atrophy and evidence for semi-dominant inheritance." Pesch U.E.A., Leo-Kottler B., Mayer S., Jurklies B., Kellner U., Apfelstedt-Sylla E., Zrenner E., Alexander C., Wissinger B. Hum. Mol. Genet. 10:1359-1368(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OPA1 LYS-270; ALA-273; GLN-290; TRP-290; VAL-438; GLU-468; CYS-551 DEL AND ARG-785, VARIANTS ASN-158; VAL-192 AND ASN-550.
[16]	"Spectrum, frequency and penetrance of OPA1 mutations in dominant optic atrophy." Toomes C., Marchbank N.J., Mackey D.A., Craig J.E., Newbury-Ecob R.A., Bennett C.P., Vize C.J., Desai S.P., Black G.C.M., Patel N., Teimory M., Markham A.F., Inglehearn C.F., Churchill A.J. Hum. Mol. Genet. 10:1369-1378(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OPA1 GLN-290; GLU-300; PHE-384; LYS-503 AND ASN-505, VARIANTS ASN-158 AND GLY-907.
[17]	"A comprehensive survey of mutations in the OPA1 gene in patients with autosomal dominant optic atrophy." Thiselton D.L., Alexander C., Taanman J.-W., Brooks S., Rosenberg T., Eiberg H., Andreasson S., Van Regemorter N., Munier F.L., Moore A.T., Bhattacharya S.S., Votruba M. Invest. Ophthalmol. Vis. Sci. 43:1715-1724(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OPA1 38-ARG--SER-43 DEL; 586-ARG--ASP-589 DEL; ARG-396; ILE-432 DEL; LYS-503 AND HIS-571, VARIANTS ASN-158; LEU-167 AND VAL-192.
[18]	"A novel mutation in the OPA1 gene in a Japanese patient with optic atrophy." Shimizu S., Mori N., Kishi M., Sugata H., Tsuda A., Kubota N. Am. J. Ophthalmol. 135:256-257(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OPA1 HIS-445.
[19]	"Fourteen novel OPA1 mutations in autosomal dominant optic atrophy including two de novo mutations in sporadic optic atrophy." Baris O., Delettre C., Amati-Bonneau P., Surget M.-O., Charlin J.-F., Catier A., Derieux L., Guyomard J.-L., Dollfus H., Jonveaux P., Ayuso C., Maumenee I., Lorenz B., Mohammed S., Tourmen Y., Bonneau D., Malthiery Y., Hamel C., Reynier P. Hum. Mutat. 21:656-656(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OPA1 PRO-272; GLY-470; PRO-574 AND 700-LEU-LYS-701 DEL.
[20]	"Dominant optic atrophy, sensorineural hearing loss, ptosis, and ophthalmoplegia: a syndrome caused by a missense mutation in OPA1." Payne M., Yang Z., Katz B.J., Warner J.E.A., Weight C.J., Zhao Y., Pearson E.D., Treft R.L., Hillman T., Kennedy R.J., Meire F.M., Zhang K. Am. J. Ophthalmol. 138:749-755(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DOA+ HIS-445.
[21]	"Dominant optic atrophy: correlation between clinical and molecular genetic studies." Puomila A., Huoponen K., Maentyjaervi M., Haemaelaeinen P., Paananen R., Sankila E.-M., Savontaus M.-L., Somer M., Nikoskelainen E. Acta Ophthalmol. Scand. 83:337-346(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OPA1 324-ARG--PRO-326 DEL; TRP-590 AND LYS-728, VARIANT ASN-158.
[22]	"OPA1 R445H mutation in optic atrophy associated with sensorineural deafness." Amati-Bonneau P., Guichet A., Olichon A., Chevrollier A., Viala F., Miot S., Ayuso C., Odent S., Arrouet C., Verny C., Calmels M.-N., Simard G., Belenguer P., Wang J., Puel J.-L., Hamel C., Malthiery Y., Bonneau D., Lenaers G., Reynier P. Ann. Neurol. 58:958-963(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DOA+ HIS-445.
[23]	"OPA1 mutations and mitochondrial DNA haplotypes in autosomal dominant optic atrophy." Han J., Thompson-Lowrey A.J., Reiss A., Mayorov V., Jia H., Biousse V., Newman N.J., Brown M.D. Genet. Med. 8:217-225(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OPA1 SER-8; CYS-80 AND CYS-841, VARIANTS ASN-158 AND VAL-192.
[24]	"Novel mutations in the OPA1 gene and associated clinical features in Japanese patients with optic atrophy." Nakamura M., Lin J., Ueno S., Asaoka R., Hirai T., Hotta Y., Miyake Y., Terasaki H. Ophthalmology 113:483-488(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OPA1 ARG-545.
[25]	"Progressive external ophthalmoplegia and vision and hearing loss in a patient with mutations in POLG2 and OPA1." Ferraris S., Clark S., Garelli E., Davidzon G., Moore S.A., Kardon R.H., Bienstock R.J., Longley M.J., Mancuso M., Gutierrez Rios P., Hirano M., Copeland W.C., DiMauro S. Arch. Neurol. 65:125-131(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DOA+ CYS-582.
[26]	"Molecular screening of 980 cases of suspected hereditary optic neuropathy with a report on 77 novel OPA1 mutations." Ferre M., Bonneau D., Milea D., Chevrollier A., Verny C., Dollfus H., Ayuso C., Defoort S., Vignal C., Zanlonghi X., Charlin J.-F., Kaplan J., Odent S., Hamel C.P., Procaccio V., Reynier P., Amati-Bonneau P. Hum. Mutat. 30:E692-E705(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OPA1 MET-95; CYS-102; 293-VAL-VAL-294 DEL; ARG-310; THR-357; MET-382; PRO-396; 429-PRO-ASN-430 DEL; ASP-430; ARG-449; 463-ILE-PHE-464 INS; LYS-487; ARG-545; TYR-551; GLN-590; PRO-593; LEU-646; ASP-768; TRP-781; TYR-823; LEU-882; PRO-887; CYS-932 AND PRO-949.
[27]	"Acute and late-onset optic atrophy due to a novel OPA1 mutation leading to a mitochondrial coupling defect." Nochez Y., Arsene S., Gueguen N., Chevrollier A., Ferre M., Guillet V., Desquiret V., Toutain A., Bonneau D., Procaccio V., Amati-Bonneau P., Pisella P.-J., Reynier P. Mol. Vis. 15:598-608(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OPA1 CYS-932.
[28]	"A novel OPA1 mutation in a Chinese family with autosomal dominant optic atrophy." Zhang J., Yuan Y., Lin B., Feng H., Li Y., Dai X., Zhou H., Dong X., Liu X.L., Guan M.X. Biochem. Biophys. Res. Commun. 419:670-675(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OPA1 ALA-400.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB011139 mRNA. Translation: BAA25493.1. HQ204906 Genomic DNA. Translation: ADP90057.1. HQ204907 Genomic DNA. Translation: ADP90065.1. HQ204908 Genomic DNA. Translation: ADP90073.1. HQ204910 Genomic DNA. Translation: ADP90089.1. HQ204911 Genomic DNA. Translation: ADP90097.1. HQ204912 Genomic DNA. Translation: ADP90105.1. HQ204913 Genomic DNA. Translation: ADP90113.1. HQ204914 Genomic DNA. Translation: ADP90121.1. HQ204917 Genomic DNA. Translation: ADP90145.1. HQ204918 Genomic DNA. Translation: ADP90153.1. HQ204920 Genomic DNA. Translation: ADP90169.1. HQ204921 Genomic DNA. Translation: ADP90177.1. HQ204922 Genomic DNA. Translation: ADP90185.1. HQ204923 Genomic DNA. Translation: ADP90193.1. HQ204924 Genomic DNA. Translation: ADP90201.1. HQ204925 Genomic DNA. Translation: ADP90209.1. HQ204926 Genomic DNA. Translation: ADP90217.1. HQ204927 Genomic DNA. Translation: ADP90225.1. HQ204929 Genomic DNA. Translation: ADP90241.1. HQ204930 Genomic DNA. Translation: ADP90249.1. HQ204932 Genomic DNA. Translation: ADP90265.1. HQ204933 Genomic DNA. Translation: ADP90273.1. HQ204934 Genomic DNA. Translation: ADP90281.1. HQ204935 Genomic DNA. Translation: ADP90289.1. HQ204936 Genomic DNA. Translation: ADP90297.1. HQ204938 Genomic DNA. Translation: ADP90313.1. HQ204939 Genomic DNA. Translation: ADP90321.1. HQ204940 Genomic DNA. Translation: ADP90329.1. HQ204941 Genomic DNA. Translation: ADP90337.1. HQ204942 Genomic DNA. Translation: ADP90345.1. HQ204943 Genomic DNA. Translation: ADP90353.1. HQ204944 Genomic DNA. Translation: ADP90361.1. HQ204945 Genomic DNA. Translation: ADP90369.1. AC048351 Genomic DNA. No translation available. AC106710 Genomic DNA. No translation available. CH471052 Genomic DNA. Translation: EAW78064.1. CH471052 Genomic DNA. Translation: EAW78071.1. BC075805 mRNA. Translation: AAH75805.1. AF416919 Genomic DNA. No translation available. AF416920 Genomic DNA. No translation available.
IPI	IPI00006721. IPI00107752.
PIR	T00336.
RefSeq	NP_056375.2. NM_015560.2.
UniGene	Hs.741294.
3D structure databases
ProteinModelPortal	O60313.
ModBase	Search...
Protein-protein interaction databases
IntAct	O60313. 6 interactions.
STRING	9606.ENSP00000354681.
Protein family/group databases
TCDB	9.B.25.2.1. mitochondrial inner/outer membrane fusion (MMF) family.
PTM databases
PhosphoSite	O60313.
Proteomic databases
PaxDb	O60313.
PRIDE	O60313.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000361908; ENSP00000354681; ENSG00000198836. ENST00000392438; ENSP00000376233; ENSG00000198836.
GeneID	4976.
KEGG	hsa:4976.
UCSC	uc003ftm.3. human.
Organism-specific databases
CTD	4976.
GeneCards	GC03P193311.
HGNC	HGNC:8140. OPA1.
HPA	HPA036926.
MIM	125250. phenotype. 165500. phenotype. 605290. gene.
neXtProt	NX_O60313.
Orphanet	3212. Autosomal dominant optic atrophy and congenital deafness. 98673. Autosomal dominant optic atrophy, classic type.
PharmGKB	PA31927.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0699.
HOGENOM	HOG000230714.
HOVERGEN	HBG019108.
Gene expression databases
ArrayExpress	O60313.
Bgee	O60313.
CleanEx	HS_OPA1.
Genevestigator	O60313.
GermOnline	ENSG00000198836. Homo sapiens.
Family and domain databases
InterPro	IPR022812. Dynamin. IPR001401. Dynamin_GTPase. [Graphical view]
PANTHER	PTHR11566. PTHR11566. 1 hit.
Pfam	PF00350. Dynamin_N. 1 hit. [Graphical view]
PRINTS	PR00195. DYNAMIN.
SMART	SM00053. DYNc. 1 hit. [Graphical view]
PROSITE	PS00410. DYNAMIN. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	OPA1. human.
GenomeRNAi	4976.
NextBio	19154.
PMAP-CutDB	O60313.
SOURCE	Search...

Entry information

Entry name

OPA1_HUMAN

Accession

Primary (citable) accession number: O60313
Secondary accession number(s): D3DNW4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 124 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.