Reviewed, UniProtKB/Swiss-Prot Q10361 (ETP1_SCHPO)

Names and origin

Protein names

Recommended name:
    Electron transfer protein 1, mitochondrial

Gene names

Name:	etp1
ORF Names:	SPAC22E12.10c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	631 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Subcellular location	Mitochondrion membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the COX15/ctaA family. Contains 1 2Fe-2S ferredoxin-type domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Membrane Mitochondrion
Domain	Transit peptide Transmembrane
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW protein complex assembly Inferred from electronic annotation. Source: InterPro transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to mitochondrial inner membrane Inferred by curator. Source: GeneDB_SPombe
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 631		Electron transfer protein 1, mitochondrial		PRO_0000006079
Regions
	Transmembrane	98 – 118	21	Potential
	Transmembrane	183 – 203	21	Potential
	Transmembrane	213 – 233	21	Potential
	Transmembrane	255 – 275	21	Potential
	Transmembrane	312 – 332	21	Potential
	Transmembrane	381 – 401	21	Potential
	Transmembrane	418 – 438	21	Potential
	Transmembrane	440 – 460	21	Potential
	Domain	519 – 621	103	2Fe-2S ferredoxin-type
Sites
	Metal binding	556	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	562	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	565	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	602	1	Iron-sulfur (2Fe-2S) By similarity
Experimental info
	Sequence conflict	94	1	P → S Ref.1
	Sequence conflict	112	1	I → T Ref.1
	Sequence conflict	443	1	A → V Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q10361-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: F936B4E56D4FF169	FASTA	631	70,147
	10 20 30 40 50 60 MNISRSSGLM RQFLLQPLRK GCDISCLGRS SWRMSRSFSG SSVLNEINLS RTKNLFLNDC 70 80 90 100 110 120 KFNKNSFEKF FARRLSNSVA PTPGGILQET EKIPSKKVAF WLLGSSALVL AIVVVGGITR 130 140 150 160 170 180 LTESGLSITE WKPITGVIPP LTDEQWNQEF ELYKKSPEFE KLNSHMTVDE FKNIFFWEWF 190 200 210 220 230 240 HRVLGRGIGL TILLPSIYMI VTKRASPWLS KRLIGLTGLV GLQGVIGWWM VKSGLSEELF 250 260 270 280 290 300 SDGSHPRVSH YRLATHLAAA VALYIGLVWT GHGILQRHAF LKSMKSGSTS QLTSMVSSVQ 310 320 330 340 350 360 KMKGFRTSVN SFVGLVLITL LSGAFVAGLD AGMIYCTFPE MGEGRLAPSK SELFDQRFCR 370 380 390 400 410 420 KDDKSDLIWR NMIDNPSLVQ LEHRILAITT FVAACGLFIF SRAKRNILPK KIKTSINVVT 430 440 450 460 470 480 GVVTAQATLG IMTLIYVVPV PLAALHQAGS LVTLTAALSL AQRLHPEYAL KNIRSWTKLI 490 500 510 520 530 540 SSPPKSSISS SILTQQRQFH TFRPSFHSEI KKPLPGTGIK VFFVTPEGRE IMIEGNEGDS 550 560 570 580 590 600 ILDLAHANNI DLEGACEGSV ACSTCHVIVD PEHYELLDPP EEDEEDMLDL AFGLEETSRL 610 620 630 GCQVLLRKDL DGIRVRIPAQ TRNIRLERPK A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Functional expression of human mitochondrial CYP11B2 in fission yeast and identification of a new internal electron transfer protein, etp1." Bureik M., Schiffler B., Hiraoka Y., Vogel F., Bernhardt R. Biochemistry 41:2311-2321(2002) [PubMed: 11841224] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, SUBCELLULAR LOCATION.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAA93897.1.
PIR	T38167.
RefSeq	NP_594836.1.
3D structure databases
HSSP	HSSP built from PDB template 1E6E based on UniProtKB P00257.
ModBase	Search...
Genome annotation databases
GeneID	2541839.
KEGG	spo:SPAC22E12.10c.
NMPDR	fig|4896.1.peg.4806.
Organism-specific databases
GeneDB_Spombe	SPAC22E12.10c.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002908-MON.
Gene expression databases
ArrayExpress	Q10361.
Family and domain databases
InterPro	IPR001055. Adrenodoxin. IPR012675. b-grasp_ferredoxin-like. IPR003780. COX15_CtaA. IPR001041. Ferredoxin. [Graphical view]
Gene3D	G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
Pfam	PF02628. COX15-CtaA. 1 hit. PF00111. Fer2. 1 hit. [Graphical view]
PRINTS	PR00355. ADRENODOXIN.
PROSITE	PS51085. 2FE2S_FER_2. 1 hit. PS00814. ADX. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ETP1_SCHPO

Accession

Primary (citable) accession number: Q10361

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 25, 2008
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)