Reviewed, UniProtKB/Swiss-Prot P10255 (CYPH_NEUCR)

Names and origin

Protein names

Recommended name:
    Peptidyl-prolyl cis-trans isomerase, mitochondrial
      Short name=PPIase
      Short name=Rotamase
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin
      Short name=CPH
    Cyclosporin A-binding protein

Gene names

ORF Names:

NCU00726

Organism

Neurospora crassa [Complete proteome]

Taxonomic identifier

5141 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

Protein attributes

Sequence length	223 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	PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.
Subcellular location	Mitochondrion. Cytoplasm.
Sequence similarities	Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Cellular component	Cytoplasm Mitochondrion
Coding sequence diversity	Alternative initiation Alternative splicing
Domain	Transit peptide
Ligand	Cyclosporin
Molecular function	Isomerase Rotamase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peptide binding Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]

Isoform Mitochondrial (identifier: P10255-1)

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 Cytosolic (identifier: P10255-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: Missing.

Note: Produced by alternative initiation.

Isoform Short (identifier: P10255-3)

The sequence of this isoform differs from the canonical sequence as follows:
     119-223: GGDFTRGNGT...KPTIVDCGAL → AAVLFVTPRSPPLSTAALSKFPCGHCRGF

Note: Produced by alternative splicing. This isoform is found in the cell following 22 hours growth in dark.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 44	44	Mitochondrion
	Chain	45 – 223	179	Peptidyl-prolyl cis-trans isomerase, mitochondrial		PRO_0000025475
Regions
	Domain	62 – 222	161	PPIase cyclophilin-type
Natural variations
	Alternative sequence	1 – 43	43	Missing in isoform Cytosolic.		VSP_018863
	Alternative sequence	119 – 223	105	GGDFT…DCGAL → AAVLFVTPRSPPLSTAALSK FPCGHCRGF in isoform Short.		VSP_029976

Sequences

	Sequence		Length	Mass (Da)
	Isoform Mitochondrial [UniParc]. Last modified July 1, 1989. Version 1. Checksum: D494AB77F9768AE0	FASTA	223	24,064
	10 20 30 40 50 60 MFGPRHFSVL KTTGSLVSST FSSSLKPTAT FSCARAFSQT SSIMSKVFFD LEWEGPVLGP 70 80 90 100 110 120 NNKPTSEIKA QSGRINFTLY DDVVPKTARN FKELCTGQNG FGYKGSSFHR IIPEFMLQGG 130 140 150 160 170 180 DFTRGNGTGG KSIYGEKFAD ENFAKKHVRP GLLSMANAGP NTNGSQFFVT TVPTSWLDGR 190 200 210 220 HVVFGEVADD ESMKVVKALE ATGSSSGAIR YSKKPTIVDC GAL
	Isoform Cytosolic. Checksum: DF4C5CFB7E2C59F3	FASTA	180	19,523
	10 20 30 40 50 60 MSKVFFDLEW EGPVLGPNNK PTSEIKAQSG RINFTLYDDV VPKTARNFKE LCTGQNGFGY 70 80 90 100 110 120 KGSSFHRIIP EFMLQGGDFT RGNGTGGKSI YGEKFADENF AKKHVRPGLL SMANAGPNTN 130 140 150 160 170 180 GSQFFVTTVP TSWLDGRHVV FGEVADDESM KVVKALEATG SSSGAIRYSK KPTIVDCGAL
	Isoform Short. Checksum: 993E29376C83382B	FASTA	147	16,083
	10 20 30 40 50 60 MFGPRHFSVL KTTGSLVSST FSSSLKPTAT FSCARAFSQT SSIMSKVFFD LEWEGPVLGP 70 80 90 100 110 120 NNKPTSEIKA QSGRINFTLY DDVVPKTARN FKELCTGQNG FGYKGSSFHR IIPEFMLQAA 130 140 VLFVTPRSPP LSTAALSKFP CGHCRGF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cyclosporin A-binding protein (cyclophilin) of Neurospora crassa. One gene codes for both the cytosolic and mitochondrial forms." Tropschug M., Nicholson D.W., Hartl F.-U., Kohler H., Pfanner N., Wachter E., Neupert W. J. Biol. Chem. 263:14433-14440(1988) [PubMed: 2971658] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CYTOSOLIC AND MITOCHONDRIAL), PARTIAL PROTEIN SEQUENCE, ALTERNATIVE INITIATION. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[2]	"Nucleotide sequence of the gene coding for cyclophilin/peptidyl-prolyl cis-trans isomerase of Neurospora crassa." Tropschug M. Nucleic Acids Res. 18:190-190(1990) [PubMed: 2137907] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The genome sequence of the filamentous fungus Neurospora crassa." Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W. Nature 422:859-868(2003) [PubMed: 12712197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J03963 mRNA. Translation: AAA33584.1. X17692 Genomic DNA. Translation: CAA35681.1. X17692 Genomic DNA. Translation: CAA35682.1. AABX02000002 Genomic DNA. Translation: EDO65376.1. AABX02000002 Genomic DNA. Translation: EDO65377.1.
PIR	CSNCM. B30809.
RefSeq	XP_001728468.1.
3D structure databases
HSSP	HSSP built from PDB template 1E3B based on UniProtKB P52011.
SMR	P10255. Positions 58-221.
ModBase	Search...
Genome annotation databases
GeneID	5847832.
NMPDR	fig|5141.1.peg.2839.
Enzyme and pathway databases
BRENDA	5.2.1.8. 266.
Family and domain databases
InterPro	IPR002130. PPIase_cyclophilin. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PRINTS	PR00153. CSAPPISMRASE.
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYPH_NEUCR

Accession

Primary (citable) accession number: P10255
Secondary accession number(s): A7UVW7, A7UVW8, Q7RV39

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	June 16, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)