Q9Y536 (PAL4A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase A-like 4A/B/C
Short name=PPIase A-like 4A
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:	PPIAL4A
Synonyms:	COAS2
AND
Name:	PPIAL4B
AND
Name:	PPIAL4C

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.
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 pleiomorphic 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.

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 4A/B/C		PRO_0000324640
Regions
	Domain	7 – 163	157	PPIase cyclophilin-type

Sequences

	Sequence		Length	Mass (Da)
	Q9Y536 [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. NM_001135789.2. NP_001137355.1. NM_001143883.2. NP_839944.1. NM_178230.1. XP_003846538.2. XM_003846490.2.
UniGene	Hs.573713. Hs.631792. Hs.717306.
3D structure databases
HSSP	HSSP built from PDB template 1W8M based on UniProtKB P62937.
ProteinModelPortal	Q9Y536.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000358224.
PTM databases
PhosphoSite	Q9Y536.
Proteomic databases
PaxDb	Q9Y536.
PRIDE	Q9Y536.
Protocols and materials databases
DNASU	164022.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000369222; ENSP00000358224; ENSG00000198161. ENST00000539781; ENSP00000439146; ENSG00000255963. ENST00000540273; ENSP00000443989; ENSG00000255854.
GeneID	100996725. 164022. 653505. 653598.
KEGG	hsa:100996725. hsa:164022. hsa:653505. hsa:653598.
UCSC	uc001ekw.3. human.
Organism-specific databases
CTD	164022. 653505. 653598.
GeneCards	GC01M144360. GC01M147954. GC01P149552.
H-InvDB	HIX0028837. HIX0159741.
HGNC	HGNC:24369. PPIAL4A. HGNC:33994. PPIAL4B. HGNC:33995. PPIAL4C.
MIM	608608. gene.
neXtProt	NX_Q9Y536.
PharmGKB	PA164724917.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0652.
HOGENOM	HOG000065981.
HOVERGEN	HBG001065.
InParanoid	Q9Y536.
KO	K12738.
OMA	ATHEPIK.
OrthoDB	EOG4DJJXN.
PhylomeDB	Q9Y536.
Gene expression databases
Bgee	Q9Y536.
Genevestigator	Q9Y536.
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
NextBio	88425.
SOURCE	Search...

Entry information

Entry name

PAL4A_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:	May 1, 2013
This is version 103 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.