Reviewed, UniProtKB/Swiss-Prot Q13356 (PPIL2_HUMAN)

Names and origin

Protein names

Recommended name:
    Peptidyl-prolyl cis-trans isomerase-like 2
      Short name=PPIase
      Short name=Rotamase
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin-60
    Cyclophilin-like protein Cyp-60

Gene names

Name:

PPIL2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	520 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.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subcellular location	Nucleus.
Tissue specificity	Highest expression in thymus, pancreas and testis. Also detected in heart, placenta, lung, liver, skeletal muscle, kidney, spleen, prostate, ovary, small intestine and colon. Poorly detected in brain and leucocytes. Strong protein expression in lymph node (cortical, paracortical and medullar regions), thyroid (follicular epithelial cells), testis (developing spermatozoa), stomach (cells lining the gastric pit), pancreas, kidney (proximal and distal-tubule cells and collecting duct cells but not in glomeruli), endometrium, and colon (goblet cells). Moderate protein expression in spleen, prostate (epithelium and squamous cell carcinoma), placenta, and adrenal gland. Weak protein expression in liver, heart, breast, ovary, and lung. No protein expression in brain and bladder. High protein expression in most lymphomas and melanomas.
Sequence similarities	Belongs to the cyclophilin-type PPIase family. PPIL2 subfamily. Contains 1 PPIase cyclophilin-type domain. Contains 1 U-box domain.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Molecular function	Isomerase Rotamase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein polyubiquitination Inferred from direct assay. Source: MGI
Cellular component	Golgi lumen Inferred from Experiment. Source: Reactome nucleus Ref.1 Traceable author statement. Source: UniProtKB ubiquitin ligase complex Inferred from electronic annotation. Source: InterPro
Molecular function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: InterPro ubiquitin-protein ligase activity Inferred from direct assay. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13356-1)

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 2 (identifier: Q13356-2)

The sequence of this isoform differs from the canonical sequence as follows:
     490-520: KRAAEEEPSTSATVPMSKKKPSRGFGDFSSW → EQQRKSPQPVPLSPCPRRSPVGVLGTSAPGSSRLPDDH

Notes: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 520

520

Peptidyl-prolyl cis-trans isomerase-like 2

PRO_0000064171

Regions

Domain

42 – 101

60

U-box

Domain

278 – 433

156

PPIase cyclophilin-type

Coiled coil

197 – 217

21

Potential

Natural variations

Alternative sequence

490 – 520

31

KRAAE…DFSSW → EQQRKSPQPVPLSPCPRRSP VGVLGTSAPGSSRLPDDH in isoform 2.

VSP_005182

Experimental info

Sequence conflict

455

1

V → I in AAH28385. Ref.3

Secondary structure

1

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520

Helix Strand Turn

Details...

Beta strand

280 – 286

7

Beta strand

289 – 295

7

Turn

297 – 299

3

Helix

301 – 312

12

Turn

313 – 318

6

Beta strand

323 – 325

3

Turn

326 – 328

3

Beta strand

329 – 332

4

Beta strand

337 – 340

4

Beta strand

365 – 368

4

Beta strand

380 – 385

6

Helix

388 – 390

3

Turn

391 – 393

3

Beta strand

396 – 402

7

Helix

404 – 412

9

Turn

417 – 419

3

Beta strand

422 – 424

3

Beta strand

427 – 435

9

Helix

439 – 455

17

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 3FFA51C3D82F0957	FASTA	520	58,823
	10 20 30 40 50 60 MGKRQHQKDK MYITCAEYTH FYGGKKPDLP QTNFRRLPFD HCSLSLQPFV YPVCTPDGIV 70 80 90 100 110 120 FDLLNIVPWL KKYGTNPSNG EKLDGRSLIK LNFSKNSEGK YHCPVLFTVF TNNTHIVAVR 130 140 150 160 170 180 TTGNVYAYEA VEQLNIKAKN FRDLLTDEPF SRQDIITLQD PTNLDKFNVS NFYHVKNNMK 190 200 210 220 230 240 IIDPDEEKAK QDPSYYLKNT NAETRETLQE LYKEFKGDEI LAATMKAPEK KKVDKLNAAH 250 260 270 280 290 300 YSTGKVSASF TSTAMVPETT HEAAAIDEDV LRYQFVKKKG YVRLHTNKGD LNLELHCDLT 310 320 330 340 350 360 PKTCENFIRL CKKHYYDGTI FHRSIRNFVI QGGDPTGTGT GGESYWGKPF KDEFRPNLSH 370 380 390 400 410 420 TGRGILSMAN SGPNSNRSQF FITFRSCAYL DKKHTIFGRV VGGFDVLTAM ENVESDPKTD 430 440 450 460 470 480 RPKEEIRIDA TTVFVDPYEE ADAQIAQERK TQLKVAPETK VKSSQPQAGS QGPQTFRQGV 490 500 510 520 GKYINPAATK RAAEEEPSTS ATVPMSKKKP SRGFGDFSSW
	Isoform 2 [UniParc]. Checksum: 9B494AE6D29EBAC3		527	59,458
	10 20 30 40 50 60 MGKRQHQKDK MYITCAEYTH FYGGKKPDLP QTNFRRLPFD HCSLSLQPFV YPVCTPDGIV 70 80 90 100 110 120 FDLLNIVPWL KKYGTNPSNG EKLDGRSLIK LNFSKNSEGK YHCPVLFTVF TNNTHIVAVR 130 140 150 160 170 180 TTGNVYAYEA VEQLNIKAKN FRDLLTDEPF SRQDIITLQD PTNLDKFNVS NFYHVKNNMK 190 200 210 220 230 240 IIDPDEEKAK QDPSYYLKNT NAETRETLQE LYKEFKGDEI LAATMKAPEK KKVDKLNAAH 250 260 270 280 290 300 YSTGKVSASF TSTAMVPETT HEAAAIDEDV LRYQFVKKKG YVRLHTNKGD LNLELHCDLT 310 320 330 340 350 360 PKTCENFIRL CKKHYYDGTI FHRSIRNFVI QGGDPTGTGT GGESYWGKPF KDEFRPNLSH 370 380 390 400 410 420 TGRGILSMAN SGPNSNRSQF FITFRSCAYL DKKHTIFGRV VGGFDVLTAM ENVESDPKTD 430 440 450 460 470 480 RPKEEIRIDA TTVFVDPYEE ADAQIAQERK TQLKVAPETK VKSSQPQAGS QGPQTFRQGV 490 500 510 520 GKYINPAATE QQRKSPQPVP LSPCPRRSPV GVLGTSAPGS SRLPDDH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c." Wang B.B., Hayenga K.J., Payan D.G., Fisher J.M. Biochem. J. 314:313-319(1996) [PubMed: 8660300] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION. Tissue: Lymphocyte.
[2]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Hippocampus and Kidney.
[4]	"Crystal structure of the human peptidylprolyl isomerase-like 2 isoform B." Structural genomics consortium (SGC) Submitted (JAN-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 280-457.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U37219 mRNA. Translation: AAC50376.1.
U37220 mRNA. Translation: AAC50377.1.
U37221 mRNA. Translation: AAC50378.1.
CR456548 mRNA. Translation: CAG30434.1.
BC028385 mRNA. Translation: AAH28385.1.
BC000022 mRNA. Translation: AAH00022.1.

PIR

S64705.

RefSeq

NP_055152.1.
NP_680480.1.
NP_680481.1.

UniGene

Hs.438587

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZKC	X-ray	1.65	A/B	280-457	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q13356.

Proteomic databases

PeptideAtlas

Q13356.

Genome annotation databases

Ensembl

ENSG00000100023. Homo sapiens. [Contig view]

GeneID

23759.

KEGG

hsa:23759.

NMPDR

fig|9606.3.peg.21326.

Organism-specific databases

H-InvDB

HIX0016279.

HGNC

HGNC:9261. PPIL2.

MIM

607588. gene.

PharmGKB

PA33588.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

Q13356.

HOVERGEN

Q13356.

Gene expression databases

CleanEx

HS_PPIL2.

GermOnline

ENSG00000100023. Homo sapiens.

Family and domain databases

InterPro

IPR002130. PPIase_cyclophilin.
IPR003613. Ubox.
[Graphical view]

Gene3D

G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.

PANTHER

PTHR11071. PPIase_cyclophilin. 1 hit.

Pfam

PF00160. Pro_isomerase. 1 hit.
[Graphical view]

PRINTS

PR00153. CSAPPISMRASE.

SMART

SM00504. Ubox. 1 hit.
[Graphical view]

PROSITE

PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

46699.

SOURCE

Search...

Entry information

Entry name

PPIL2_HUMAN

Accession

Primary (citable) accession number: Q13356
Secondary accession number(s): Q13357, Q8TAH2, Q9BWR8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	November 1, 1996
Last modified:	November 25, 2008
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)