Reviewed, UniProtKB/Swiss-Prot Q9Y536 (PAL4B_HUMAN)

Names and origin

Protein names

Recommended name:
    Peptidylprolyl cis-trans isomerase A-like 4B
      Short name=PPIase A-like 4B
    EC=5.2.1.8
Alternative name(s):
    Chromosome 1-amplified sequence 2
      Short name=COAS-2
    Cyclophilin homolog overexpressed in liver cancer

Gene names

Name:	PPIAL4B
Synonyms:	COAS2
AND
Name:	PPIAL4C
AND
Name:	PPIAL4D

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	164 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 By similarity.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Highly expressed in brain, ovary and mammary gland. Moderately expressed in lung, salivary gland, kidney, skin, adipose tissue, intestine and spleen. Weakly expressed in skeletal muscle, liver and stomach. Expressed in pleomorphic and undifferentiated liposarcomas, osteosarcomas and breast carcinomas. Ref.3
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.
Caution	Expression studies do not distinguish between PPIAL4B and PPIAL4 (Ref.3).

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Isomerase Rotamase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
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	Peptidylprolyl cis-trans isomerase A-like 4B		PRO_0000324640
Regions
	Domain	7 – 163	157	PPIase cyclophilin-type

Sequences

	Sequence		Length	Mass (Da)
	Q9Y536-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 99D50A72B0896C4C	FASTA	164	18,182
	10 20 30 40 50 60 MVNSVVFFDI TVDGKPLGRI SIKLFADKIL KTAENFRALS TGEKGFRYKG SCFHRIIPGF 70 80 90 100 110 120 MCQGGDFTRH NGTGDKSIYG EKFDDENLIR KHTGSGILSM ANAGPNTNGS QFFICAAKTE 130 140 150 160 WLDGKHVAFG KVKERVNIVE AMEHFGYRNS KTSKKITIAD CGQF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cyclophilin homologue overexpressed in liver cancer." Tanaka S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Positional cloning identifies a novel cyclophilin as a candidate amplified oncogene in 1q21." Meza-Zepeda L.A., Forus A., Lygren B., Dahlberg A.B., Godager L.H., South A.P., Marenholz I., Lioumi M., Florenes V.A., Maelandsmo G.M., Serra M., Mischke D., Nizetic D., Ragoussis J., Tarkkanen M., Nesland J.M., Knuutila S., Myklebost O. Oncogene 21:2261-2269(2002) [PubMed: 11948409] [Abstract] Cited for: TISSUE SPECIFICITY.
[4]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB084917 mRNA. Translation: BAB92073.1. AL022240 Genomic DNA. Translation: CAB46877.1. AL451058 Genomic DNA. Translation: CAH71953.1. BX248398 Genomic DNA. Translation: CAI18814.1.
IPI	IPI00030144.
RefSeq	NP_001129261.1. NP_001137355.1. NP_839944.1.
UniGene	Hs.573713
3D structure databases
HSSP	HSSP built from PDB template 1E3B based on UniProtKB P52011.
SMR	Q9Y536. Positions 1-164.
ModBase	Search...
Proteomic databases
PRIDE	Q9Y536.
Genome annotation databases
Ensembl	ENSG00000198161. Homo sapiens. [Contig view]
GeneID	164022. 653505. 653598.
KEGG	hsa:164022. hsa:653505. hsa:653598.
UCSC	uc001ekw.1. human.
Organism-specific databases
GeneCards	GC01M143073. GC01M146419. GC01M146569. GC01P147821.
MIM	608608. gene.
Phylogenomic databases
HOGENOM	Q9Y536.
HOVERGEN	Q9Y536.
OMA	Q9Y536. NFAHLAN.
Enzyme and pathway databases
BRENDA	5.2.1.8. 247.
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...
Other Resources
NextBio	88425.
SOURCE	Search...

Entry information

Entry name

PAL4B_HUMAN

Accession

Primary (citable) accession number: Q9Y536

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	November 1, 1999
Last modified:	July 7, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)