Reviewed, UniProtKB/Swiss-Prot Q9H2H8 (PPIL3_HUMAN)

Names and origin

Protein names

Recommended name:
    Peptidyl-prolyl cis-trans isomerase-like 3
      Short name=PPIase
      Short name=Rotamase
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin-like protein PPIL3
    Cyclophilin J
      Short name=CyPJ

Gene names

Name:

PPIL3

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	161 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. May be involved in pre-mRNA splicing.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subunit structure	Identified in the spliceosome C complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8.
Tissue specificity	Ubiquitous. Detected at low levels. Ref.1
Sequence similarities	Belongs to the cyclophilin-type PPIase family. PPIL3 subfamily. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Spliceosome
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Isomerase Rotamase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	spliceosomal complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
VP3	Q99152	1	EBI-751051,EBI-1776808	From a different organism.

Alternative products

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

Isoform 1 (identifier: Q9H2H8-1)

Also known as: PPIL3b;

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: Q9H2H8-2)

Also known as: PPIL3a;

The sequence of this isoform differs from the canonical sequence as follows:
     27-58: NFLALCASNYYNGCIFHRNIKGFMVQTGDPTG → MESRCVPQAGVQWRDLGSLQPPPPGFKQVFCLSLPR

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 161

161

Peptidyl-prolyl cis-trans isomerase-like 3

PRO_0000064166

Regions

Domain

1 – 154

154

PPIase cyclophilin-type

Natural variations

Alternative sequence

27 – 58

32

NFLAL…GDPTG → MESRCVPQAGVQWRDLGSLQ PPPPGFKQVFCLSLPR in isoform 2.

VSP_015468

Natural variant

146

1

D → E: dbSNP rs7562391. Ref.5

VAR_023417

Experimental info

Sequence conflict

61 – 62

2

RG → KR in AAO64723. Ref.2

Sequence conflict

65

1

S → V in AAO64723. Ref.2

Sequence conflict

78

1

Y → I in AAO64723. Ref.2

Secondary structure

1

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161

Helix Strand Turn

Details...

Beta strand

2 – 7

6

Beta strand

10 – 16

7

Turn

18 – 20

3

Helix

22 – 33

12

Turn

34 – 39

6

Beta strand

44 – 46

3

Turn

47 – 49

3

Beta strand

50 – 53

4

Beta strand

58 – 61

4

Beta strand

86 – 89

4

Beta strand

92 – 95

4

Beta strand

101 – 106

6

Helix

109 – 111

3

Turn

112 – 114

3

Beta strand

117 – 123

7

Helix

125 – 132

8

Turn

138 – 140

3

Beta strand

143 – 145

3

Beta strand

148 – 155

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (PPIL3b) [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 5FE190D7858B07D4	FASTA	161	18,155
	10 20 30 40 50 60 MSVTLHTDVG DIKIEVFCER TPKTCENFLA LCASNYYNGC IFHRNIKGFM VQTGDPTGTG 70 80 90 100 110 120 RGGNSIWGKK FEDEYSEYLK HNVRGVVSMA NNGPNTNGSQ FFITYGKQPH LDMKYTVFGK 130 140 150 160 VIDGLETLDE LEKLPVNEKT YRPLNDVHIK DITIHANPFA Q
	Isoform 2 (PPIL3a). Checksum: A533E5F757C18934	FASTA	165	18,627
	10 20 30 40 50 60 MSVTLHTDVG DIKIEVFCER TPKTCEMESR CVPQAGVQWR DLGSLQPPPP GFKQVFCLSL 70 80 90 100 110 120 PRTGRGGNSI WGKKFEDEYS EYLKHNVRGV VSMANNGPNT NGSQFFITYG KQPHLDMKYT 130 140 150 160 VFGKVIDGLE TLDELEKLPV NEKTYRPLND VHIKDITIHA NPFAQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of a novel peptidylprolyl isomerase (cyclophilin)-like gene (PPIL3) from human fetal brain." Zhou Z., Ying K., Dai J., Tang R., Wang W., Huang Y., Zhao W., Xie Y., Mao Y. Cytogenet. Cell Genet. 92:231-236(2001) [PubMed: 11435694] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY. Tissue: Fetal brain.
[2]	Ding J.B., Yu L., Zhao S.Y. Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Embryo.
[4]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORM 1), VARIANT GLU-146. Tissue: Placenta.
[6]	"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis." Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J. RNA 8:426-439(2002) [PubMed: 11991638] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPICEOSOMAL C COMPLEX.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"Structure of recombinant human cyclophilin J, a novel member of the cyclophilin family." Huang L.-L., Zhao X.-M., Huang C.-Q., Yu L., Xia Z.-X. Acta Crystallogr. D 61:316-321(2005) [PubMed: 15735342] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF251049 mRNA. Translation: AAK34939.1.
AF271652 mRNA. Translation: AAG44766.1.
AF146799 mRNA. Translation: AAO64723.1.
AK027315 mRNA. Translation: BAB55036.1.
AC005037 Genomic DNA. Translation: AAY14723.1.
BC007693 mRNA. Translation: AAH07693.1.

IPI

IPI00032473.
IPI00300952.

RefSeq

NP_115861.1.
NP_570981.1.
NP_572028.1.

UniGene

Hs.121076

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XYH	X-ray	2.60	A	1-161	[»]
2OJU	X-ray	2.40	A/B	1-161	[»]
2OK3	X-ray	2.00	A	1-161	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H2H8. 2 interactions.

STRING

Q9H2H8.

Proteomic databases

PRIDE

Q9H2H8.

Genome annotation databases

Ensembl

ENST00000234288; ENSP00000234288; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000286175; ENSP00000286175; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000321356; ENSP00000326830; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000334509; ENSP00000334569; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000357369; ENSP00000349935; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000392283; ENSP00000376107; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000409264; ENSP00000386893; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000409361; ENSP00000386235; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000409403; ENSP00000386875; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000409449; ENSP00000387012; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000409769; ENSP00000386358; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000415562; ENSP00000400726; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000422134; ENSP00000400192; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000432425; ENSP00000400487; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000434813; ENSP00000394734; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000443398; ENSP00000391082; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000457063; ENSP00000401196; ENSG00000013441; Homo sapiens. [Genome view]

GeneID

53938.

KEGG

hsa:53938.

UCSC

uc002uwh.1. human.
uc002uwi.1. human.

Organism-specific databases

CTD

53938.

GeneCards

GC02M201443.

H-InvDB

HIX0002729.

HGNC

HGNC:9262. PPIL3.

PharmGKB

PA33589.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9H2H8.

OMA

ACENFLA.

Enzyme and pathway databases

BRENDA

5.2.1.8. 247.

Gene expression databases

ArrayExpress

Q9H2H8.

Bgee

Q9H2H8.

CleanEx

HS_PPIL3.

Genevestigator

Q9H2H8.

GermOnline

ENSG00000115934. Homo sapiens.

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

56240.

Entry information

Entry name

PPIL3_HUMAN

Accession

Primary (citable) accession number: Q9H2H8
Secondary accession number(s): Q86WF9, Q96IA9, Q9BXZ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	March 1, 2001
Last modified:	November 3, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.