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F5H284 (PAL4D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase A-like 4D

Short name=PPIase A-like 4D
EC=5.2.1.8
Gene names
Name:PPIAL4D
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length164 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Subcellular location

Cytoplasm By similarity.

Miscellaneous

It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 1.

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIase A subfamily.

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionIsomerase
Rotamase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

protein peptidyl-prolyl isomerization

Inferred from electronic annotation. Source: GOC

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 164164Peptidyl-prolyl cis-trans isomerase A-like 4D
PRO_0000420907

Regions

Domain7 – 163157PPIase cyclophilin-type

Sequences

Sequence LengthMass (Da)Tools
F5H284 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: 647DF57F1A6FC81E

FASTA16418,167
        10         20         30         40         50         60 
MVNSVVFFEI TRDGKPLGRI SIKLFADKIP KTAENFRALS TGEKGFRYKG SCFHRIIPGF 

        70         80         90        100        110        120 
MCQGGDFTRP NGTGDKSIYG EKFDDENLIR KHTGSGILSM ANAGPNTNGS QFFICAAKTE 

       130        140        150        160 
WLDGKHVAFG KVKERVNIVE ATEHFGYRNS KTSKKITIAD CGQF 

« Hide

References

[1]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX283067 Genomic DNA. No translation available.
IPIIPI00455871.
RefSeqNP_001137504.1. NM_001144032.1.
NP_001157733.1. NM_001164261.1.
NP_001157734.1. NM_001164262.1.

3D structure databases

ProteinModelPortalF5H284.
SMRF5H284. Positions 2-164.
ModBaseSearch...

PTM databases

PhosphoSiteF5H284.

Proteomic databases

PRIDEF5H284.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000544708; ENSP00000439444; ENSG00000256374.
ENST00000583898; ENSP00000464608; ENSG00000269573.
GeneID645142.
728945.
730262.
KEGGhsa:645142.
hsa:728945.
hsa:730262.
UCSCuc010pag.2. human.

Organism-specific databases

CTD645142.
728945.
730262.
GeneCardsGC01M148202.
HGNCHGNC:33998. PPIAL4D.
neXtProtNX_F5H284.
GenAtlasSearch...

Phylogenomic databases

KOK12738.
OMAIVEATEH.

Family and domain databases

InterProIPR002130. Cyclophilin-like_PPIase_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. CSA_PPIase. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio117124.

Entry information

Entry namePAL4D_HUMAN
AccessionPrimary (citable) accession number: F5H284
Entry history
Integrated into UniProtKB/Swiss-Prot: February 6, 2013
Last sequence update: June 28, 2011
Last modified: May 1, 2013
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

SIMILARITY comments

Index of protein domains and families