A2BFH1 (PAL4G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase A-like 4G
Short name=PPIase A-like 4G
EC=5.2.1.8

Alternative name(s):
Peptidylprolyl cis-trans isomerase A-like 4

Gene names

Name:

PPIAL4G

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	164 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

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 component	Cytoplasm
Molecular function	Isomerase Rotamase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein peptidyl-prolyl isomerization Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	peptidyl-prolyl cis-trans isomerase activity 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
	Chain	1 – 164	164	Peptidyl-prolyl cis-trans isomerase A-like 4G		PRO_0000324639
Regions
	Domain	7 – 163	157	PPIase cyclophilin-type
Experimental info
	Sequence conflict	6	1	I → V in AAI30379. Ref.2
	Sequence conflict	6	1	I → V in AAI30377. Ref.2
	Sequence conflict	24	1	Q → L in AAI30379. Ref.2
	Sequence conflict	24	1	Q → L in AAI30377. Ref.2
	Sequence conflict	69	1	H → R in AAI30379. Ref.2
	Sequence conflict	69	1	H → R in AAI30377. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	A2BFH1 [UniParc]. Last modified February 20, 2007. Version 1. Checksum: CEAFE5FE3D858213	FASTA	164	18,166
	10 20 30 40 50 60 MVNSVIFFDI TVDGKPLGRI SIKQFADKIP KTAENFRALS TGEKGFRYKG SCFHRIIPGF 70 80 90 100 110 120 MCQGGDFTHP NGTGDKSIYG EKFDDENLIR KHTGSGILSM ANAGPNTNGS QFFICTAKTE 130 140 150 160 WLDGKHVAFG KVKERVNIVE AMEHFGYRNS KTSKKITIAD CGQF

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. , 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].

[2]

"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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX284650 Genomic DNA. Translation: CAM26887.1. BC130376 mRNA. Translation: AAI30377.1. BC130378 mRNA. Translation: AAI30379.1.
IPI	IPI00657716.
RefSeq	NP_001116540.1. NM_001123068.1.
UniGene	Hs.534674. Hs.573713.
3D structure databases
ProteinModelPortal	A2BFH1.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000393845.
PTM databases
PhosphoSite	A2BFH1.
Proteomic databases
PaxDb	A2BFH1.
PRIDE	A2BFH1.
Protocols and materials databases
DNASU	644591.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000419275; ENSP00000393845; ENSG00000236334.
GeneID	644591.
KEGG	hsa:644591.
UCSC	uc001ejt.3. human.
Organism-specific databases
CTD	644591.
GeneCards	GC01M143767.
HGNC	HGNC:33996. PPIAL4G.
neXtProt	NX_A2BFH1.
PharmGKB	PA164724931.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0652.
HOGENOM	HOG000065981.
HOVERGEN	HBG001065.
InParanoid	A2BFH1.
KO	K12738.
OMA	DHVERIT.
OrthoDB	EOG405S32.
Gene expression databases
Bgee	A2BFH1.
CleanEx	HS_PPIAL4A.
Genevestigator	A2BFH1.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. IPR024936. Cyclophilin-type_PPIase. IPR020892. Cyclophilin-type_PPIase_CS. [Graphical view]
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PIRSF	PIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTS	PR00153. CSAPPISMRASE.
SUPFAM	SSF50891. CSA_PPIase. 1 hit.
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	644591.
NextBio	116407.

Entry information

Entry name

PAL4G_HUMAN

Accession

Primary (citable) accession number: A2BFH1
Secondary accession number(s): A1L431

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	February 20, 2007
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 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.