[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND VARIANT ALA-301. TISSUE=Fibrosarcoma; PubMed=8723724 [NCBI, ExPASy, EBI, Israel, Japan] Ansari-Lari M.A., Muzny D.M., Lu J., Lu F., Lilley C.E., Spanos S., Malley T., Gibbs R.A.; "A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13."; Genome Res. 6:314-326(1996).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=9074930 [NCBI, ExPASy, EBI, Israel, Japan] Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.; "Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination."; Genome Res. 7:268-280(1997).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). DOI=10.1016/j.bbrc.2004.03.060; PubMed=15063763 [NCBI, ExPASy, EBI, Israel, Japan] Jaernum S., Kjellman C., Darabi A., Nilsson I., Edvardsen K., Aaman P.; "LEPREL1, a novel ER and Golgi resident member of the Leprecan family."; Biochem. Biophys. Res. Commun. 317:342-351(2004).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 54-736 (ISOFORM 1), AND VARIANT THR-685. TISSUE=Eye, and Uterus; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

Comments

FUNCTION: Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly-sequences in collagens, especially types IV and V (By similarity).
CATALYTIC ACTIVITY: Procollagen L-proline + 2-oxoglutarate + O₂ = procollagen trans-3-hydroxy-L-proline + succinate + CO₂.
COFACTOR: Iron (By similarity).
COFACTOR: Ascorbate (By similarity).
SUBCELLULAR LOCATION: Endoplasmic reticulum (By similarity).

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q8IVL6-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q8IVL6-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_019352.

TISSUE SPECIFICITY: Weak expression in heart, lung, ovary and skeletal muscle.
SIMILARITY: Belongs to the leprecan family.
SIMILARITY: Contains 1 PKHD (prolyl/lysyl hydroxylase) domain.
SIMILARITY: Contains 4 TPR repeats.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U47924; AAB51312.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U47926; AAC50464.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ430349; CAD23037.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC017217; AAH17217.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC067251; AAH67251.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC080630; AAH80630.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_055077.2; -.

UniGene

Hs.631655

3D structure databases

ModBase

Q8IVL6.

Organism-specific databases

GC12P006807; -.

HGNC:19318; LEPREL2.

610342; gene. [NCBI / EBI]

PharmGKB

PA134890414; -.

GeneCards

Q8IVL6.

Gene expression databases

ArrayExpress

Q8IVL6; -.

CleanEx

HS_LEPREL2; -.

GermOnline

ENSG00000110811; Homo sapiens.

Ontologies

GO:0005783;	Cellular component: endoplasmic reticulum (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0031418;	Molecular function: L-ascorbic acid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016702;	Molecular function: oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen (inferred from electronic annotation from UniProtKB-KW).
GO:0019797;	Molecular function: procollagen-proline 3-dioxygenase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019538;	Biological process: protein metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR005123; 2OG-FeII_Oase.
IPR000886; ER_targeting_sequence.
IPR006620; Pro_4_hyd_alph.
IPR013026; TPR_region.
Graphical view of domain structure.

Pfam

PF03171; 2OG-FeII_Oxy; 1.
Pfam graphical view of domain structure.

SMART

SM00702; P4Hc; 1.
SMART graphical view of domain structure.

PROSITE

PS00014; ER_TARGET; 1.
PS50005; TPR; FALSE_NEG.
PS50293; TPR_REGION; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).

Proteomics databases

PRIDE

Q8IVL6; -.

Genome annotation databases

Ensembl

ENSG00000110811; Homo sapiens. [Contig view]

GeneID

10536; -.

KEGG

hsa:10536; -.

Phylogenomic databases

HOGENOM

Q8IVL6; -.

HOVERGEN

Q8IVL6; -.

Other

DrugBank

DB00172; L-Proline.
DB00139; Succinic acid.
DB00126; Vitamin C.

NextBio

39973; -.

SOURCE

LEPREL2; Homo sapiens.

ProtoNet

Q8IVL6.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Coiled coil; Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Metal-binding; Oxidoreductase; Polymorphism; Repeat; Signal; TPR repeat; Vitamin C.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 20`	`20`	`Potential.`
`CHAIN`	`21 736`	`716`	`Prolyl 3-hydroxylase 3.`	`PRO_0000240360`
`REPEAT`	`37 70`	`34`	`TPR 1.`
`REPEAT`	`154 187`	`34`	`TPR 2.`
`REPEAT`	`216 249`	`34`	`TPR 3.`
`REPEAT`	`316 349`	`34`	`TPR 4.`
`DOMAIN`	`464 674`	`211`	`PKHD.`
`COILED`	`681 709`	`29`	`Potential.`
`MOTIF`	`733 736`	`4`	`Prevents secretion from ER (Potential).`
`COMPBIAS`	`173 177`	`5`	`Poly-Ala.`
`COMPBIAS`	`267 270`	`4`	`Poly-Glu.`
`COMPBIAS`	`696 704`	`9`	`Poly-Glu.`
`ACT_SITE`	`666 666`		`By similarity.`
`METAL`	`584 584`		`Iron.`
`METAL`	`586 586`		`Iron.`
`METAL`	`656 656`		`Iron.`
`CARBOHYD`	`331 331`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`462 462`		`N-linked (GlcNAc...) (Potential).`
`VAR_SEQ`	`1 185`		`Missing (in isoform 2).`	`VSP_019352`
`VARIANT`	`301 301`	`1`	`T -> A (in dbSNP:rs10744716 [NCBI]).`	`VAR_050443`
`VARIANT`	`304 304`	`1`	`R -> C (in dbSNP:rs35359746 [NCBI]).`	`VAR_050444`
`VARIANT`	`385 385`	`1`	`G -> E (in dbSNP:rs1047771 [NCBI]).`	`VAR_050445`
`VARIANT`	`685 685`	`1`	`I -> T (in dbSNP:rs1129649 [NCBI]).`	`VAR_050446`
`VARIANT`	`705 705`	`1`	`M -> T (in dbSNP:rs3213431 [NCBI]).`	`VAR_050447`
`CONFLICT`	`79 82`		`ASCA -> RTRG (in Ref. 4; AAH67251).`

Sequence information

Length: 736 AA [This is the length of the unprocessed precursor]

Molecular weight: 81837 Da [This is the MW of the unprocessed precursor]

CRC64: 82526D30C9788369 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLRLLRPLLL LLLLPPPGSP EPPGLTQLSP GAPPQAPDLL YADGLRAYAA GAWAPAVALL 

        70         80         90        100        110        120 
REALRSQAAL GRVRLDCGAS CAADPGAALP AVLLGAPEPD SGPGPTQGSW ERQLLRAALR 

       130        140        150        160        170        180 
RADCLTQCAA RRLGPGGAAR LRVGSALRDA FRRREPYNYL QRAYYQLKKL DLAAAAAHTF 

       190        200        210        220        230        240 
FVANPMHLQM REDMAKYRRM SGVRPQSFRD LETPPHWAAY DTGLELLGRQ EAGLALPRLE 

       250        260        270        280        290        300 
EALQGSLAQM ESCRADCEGP EEQQGAEEEE DGAASQGGLY EAIAGHWIQV LQCRQRCVGE 

       310        320        330        340        350        360 
TATRPGRSFP VPDFLPNQLR RLHEAHAQVG NLSQAIENVL SVLLFYPEDE AAKRALNQYQ 

       370        380        390        400        410        420 
AQLGEPRPGL GPREDIQRFI LRSLGEKRQL YYAMEHLGTS FKDPDPWTPA ALIPEALREK 

       430        440        450        460        470        480 
LREDQEKRPW DHEPVKPKPL TYWKDVLLLE GVTLTQDSRQ LNGSERAVLD GLLTPAECGV 

       490        500        510        520        530        540 
LLQLAKDAAG AGARSGYRGR RSPHTPHERF EGLTVLKAAQ LARAGTVGSQ GAKLLLEVSE 

       550        560        570        580        590        600 
RVRTLTQAYF SPERPLHLSF THLVCRSAIE GEQEQRMDLS HPVHADNCVL DPDTGECWRE 

       610        620        630        640        650        660 
PPAYTYRDYS GLLYLNDDFQ GGDLFFTEPN ALTVTARVRP RCGRLVAFSS GVENPHGVWA 

       670        680        690        700        710        720 
VTRGRRCALA LWHTWAPEHR EQEWIEAKEL LQESQEEEEE EEEEMPSKDP SPEPPSRRHQ 

       730 
RVQDKTGRAP RVREEL

Q8IVL6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools