O15296 (LX15B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arachidonate 15-lipoxygenase B
Short name=15-LOX-B
EC=1.13.11.33

Alternative name(s):
15-lipoxygenase 2
Short name=15-LOX-2
Arachidonate 15-lipoxygenase type II

Gene names

Name:

ALOX15B

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	676 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Converts arachidonic acid exclusively to 15S-hydroperoxyeicosatetraenoic acid, while linoleic acid is less well metabolized.
Catalytic activity	Arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate.
Cofactor	Binds 1 iron ion per subunit By similarity.
Pathway	Lipid metabolism; leukotriene D4 biosynthesis.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Expressed in hair, prostate, lung and cornea.
Sequence similarities	Belongs to the lipoxygenase family. Contains 1 lipoxygenase domain. Contains 1 PLAT domain.
Sequence caution	The sequence AAD37786.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Leukotriene biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	induction of apoptosis Traceable author statement Ref.3. Source: UniProtKB leukotriene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell cycle Inferred from direct assay Ref.3. Source: UniProtKB negative regulation of cell migration Traceable author statement Ref.3. Source: UniProtKB negative regulation of cell proliferation Inferred from direct assay Ref.3. Source: UniProtKB negative regulation of growth Inferred from direct assay Ref.3. Source: UniProtKB prostate gland development Non-traceable author statement Ref.3. Source: UniProtKB regulation of epithelial cell differentiation Non-traceable author statement Ref.3. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	arachidonate 15-lipoxygenase activity Inferred from direct assay Ref.3. Source: UniProtKB iron ion binding Inferred from electronic annotation. Source: InterPro lipoxygenase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: O15296-1)

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 B (identifier: O15296-2)

Also known as: 15-LOX2sv-b;

The sequence of this isoform differs from the canonical sequence as follows:
     401-429: Missing.
     483-527: Missing.

Isoform C (identifier: O15296-3)

Also known as: 15-LOX2sv-c;

The sequence of this isoform differs from the canonical sequence as follows:
     561-617: FDSCAWMPNL...WLLSKEPGDQ → VRKGQRPRWQ...PKAWQHARAS
     618-676: Missing.

Isoform D (identifier: O15296-4)

Also known as: 15-LOX2sv-a;

The sequence of this isoform differs from the canonical sequence as follows:
     401-429: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 676	676	Arachidonate 15-lipoxygenase B		PRO_0000220700
Regions
	Domain	2 – 124	123	PLAT
	Domain	125 – 676	552	Lipoxygenase
Sites
	Metal binding	373	1	Iron; catalytic By similarity
	Metal binding	378	1	Iron; catalytic By similarity
	Metal binding	553	1	Iron; catalytic By similarity
	Metal binding	676	1	Iron; via carboxylate; catalytic By similarity
Natural variations
	Alternative sequence	401 – 429	29	Missing in isoform B and isoform D.		VSP_003142
	Alternative sequence	483 – 527	45	Missing in isoform B.		VSP_003143
	Alternative sequence	561 – 617	57	FDSCA…EPGDQ → VRKGQRPRWQAGGDPAPQPH SALSAFSLTPVLGCPTCHPA CSCHHPPPKAWQHARAS in isoform C.		VSP_003144
	Alternative sequence	618 – 676	59	Missing in isoform C.		VSP_003145
	Natural variant	486	1	R → H. Ref.3 Corresponds to variant rs9895916 [ dbSNP | Ensembl ].		VAR_061334
	Natural variant	656	1	Q → R. Ref.1 Ref.2 Ref.3 Ref.6 Corresponds to variant rs4792147 [ dbSNP | Ensembl ].		VAR_024524
	Natural variant	676	1	I → V. Corresponds to variant rs7225107 [ dbSNP | Ensembl ].		VAR_024525
Experimental info
	Sequence conflict	271	1	V → L in AAB61706. Ref.1
	Sequence conflict	271	1	V → L in CAC34521. Ref.2
	Sequence conflict	338	1	G → C in AAD37786. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified January 11, 2011. Version 3. Checksum: 4F641DF2F9D492C6	FASTA	676	75,857
	10 20 30 40 50 60 MAEFRVRVST GEAFGAGTWD KVSVSIVGTR GESPPLPLDN LGKEFTAGAE EDFQVTLPED 70 80 90 100 110 120 VGRVLLLRVH KAPPVLPLLG PLAPDAWFCR WFQLTPPRGG HLLFPCYQWL EGAGTLVLQE 130 140 150 160 170 180 GTAKVSWADH HPVLQQQRQE ELQARQEMYQ WKAYNPGWPH CLDEKTVEDL ELNIKYSTAK 190 200 210 220 230 240 NANFYLQAGS AFAEMKIKGL LDRKGLWRSL NEMKRIFNFR RTPAAEHAFE HWQEDAFFAS 250 260 270 280 290 300 QFLNGLNPVL IRRCHYLPKN FPVTDAMVAS VLGPGTSLQA ELEKGSLFLV DHGILSGIQT 310 320 330 340 350 360 NVINGKPQFS AAPMTLLYQS PGCGPLLPLA IQLSQTPGPN SPIFLPTDDK WDWLLAKTWV 370 380 390 400 410 420 RNAEFSFHEA LTHLLHSHLL PEVFTLATLR QLPHCHPLFK LLIPHTRYTL HINTLARELL 430 440 450 460 470 480 IVPGQVVDRS TGIGIEGFSE LIQRNMKQLN YSLLCLPEDI RTRGVEDIPG YYYRDDGMQI 490 500 510 520 530 540 WGAVERFVSE IIGIYYPSDE SVQDDRELQA WVREIFSKGF LNQESSGIPS SLETREALVQ 550 560 570 580 590 600 YVTMVIFTCS AKHAAVSAGQ FDSCAWMPNL PPSMQLPPPT SKGLATCEGF IATLPPVNAT 610 620 630 640 650 660 CDVILALWLL SKEPGDQRPL GTYPDEHFTE EAPRRSIATF QSRLAQISRG IQERNQGLVL 670 PYTYLDPPLI ENSVSI
	Isoform B (15-LOX2sv-b) [UniParc]. Checksum: 8804BB44095695C2	FASTA	602	67,345
	10 20 30 40 50 60 MAEFRVRVST GEAFGAGTWD KVSVSIVGTR GESPPLPLDN LGKEFTAGAE EDFQVTLPED 70 80 90 100 110 120 VGRVLLLRVH KAPPVLPLLG PLAPDAWFCR WFQLTPPRGG HLLFPCYQWL EGAGTLVLQE 130 140 150 160 170 180 GTAKVSWADH HPVLQQQRQE ELQARQEMYQ WKAYNPGWPH CLDEKTVEDL ELNIKYSTAK 190 200 210 220 230 240 NANFYLQAGS AFAEMKIKGL LDRKGLWRSL NEMKRIFNFR RTPAAEHAFE HWQEDAFFAS 250 260 270 280 290 300 QFLNGLNPVL IRRCHYLPKN FPVTDAMVAS VLGPGTSLQA ELEKGSLFLV DHGILSGIQT 310 320 330 340 350 360 NVINGKPQFS AAPMTLLYQS PGCGPLLPLA IQLSQTPGPN SPIFLPTDDK WDWLLAKTWV 370 380 390 400 410 420 RNAEFSFHEA LTHLLHSHLL PEVFTLATLR QLPHCHPLFK STGIGIEGFS ELIQRNMKQL 430 440 450 460 470 480 NYSLLCLPED IRTRGVEDIP GYYYRDDGMQ IWGIPSSLET REALVQYVTM VIFTCSAKHA 490 500 510 520 530 540 AVSAGQFDSC AWMPNLPPSM QLPPPTSKGL ATCEGFIATL PPVNATCDVI LALWLLSKEP 550 560 570 580 590 600 GDQRPLGTYP DEHFTEEAPR RSIATFQSRL AQISRGIQER NQGLVLPYTY LDPPLIENSV SI
	Isoform C (15-LOX2sv-c) [UniParc]. Checksum: 3F690488B2B766AC	FASTA	617	69,136
	10 20 30 40 50 60 MAEFRVRVST GEAFGAGTWD KVSVSIVGTR GESPPLPLDN LGKEFTAGAE EDFQVTLPED 70 80 90 100 110 120 VGRVLLLRVH KAPPVLPLLG PLAPDAWFCR WFQLTPPRGG HLLFPCYQWL EGAGTLVLQE 130 140 150 160 170 180 GTAKVSWADH HPVLQQQRQE ELQARQEMYQ WKAYNPGWPH CLDEKTVEDL ELNIKYSTAK 190 200 210 220 230 240 NANFYLQAGS AFAEMKIKGL LDRKGLWRSL NEMKRIFNFR RTPAAEHAFE HWQEDAFFAS 250 260 270 280 290 300 QFLNGLNPVL IRRCHYLPKN FPVTDAMVAS VLGPGTSLQA ELEKGSLFLV DHGILSGIQT 310 320 330 340 350 360 NVINGKPQFS AAPMTLLYQS PGCGPLLPLA IQLSQTPGPN SPIFLPTDDK WDWLLAKTWV 370 380 390 400 410 420 RNAEFSFHEA LTHLLHSHLL PEVFTLATLR QLPHCHPLFK LLIPHTRYTL HINTLARELL 430 440 450 460 470 480 IVPGQVVDRS TGIGIEGFSE LIQRNMKQLN YSLLCLPEDI RTRGVEDIPG YYYRDDGMQI 490 500 510 520 530 540 WGAVERFVSE IIGIYYPSDE SVQDDRELQA WVREIFSKGF LNQESSGIPS SLETREALVQ 550 560 570 580 590 600 YVTMVIFTCS AKHAAVSAGQ VRKGQRPRWQ AGGDPAPQPH SALSAFSLTP VLGCPTCHPA 610 CSCHHPPPKA WQHARAS
	Isoform D (15-LOX2sv-a) [UniParc]. Checksum: EE51EEA9221CCC4B	FASTA	647	72,523
	10 20 30 40 50 60 MAEFRVRVST GEAFGAGTWD KVSVSIVGTR GESPPLPLDN LGKEFTAGAE EDFQVTLPED 70 80 90 100 110 120 VGRVLLLRVH KAPPVLPLLG PLAPDAWFCR WFQLTPPRGG HLLFPCYQWL EGAGTLVLQE 130 140 150 160 170 180 GTAKVSWADH HPVLQQQRQE ELQARQEMYQ WKAYNPGWPH CLDEKTVEDL ELNIKYSTAK 190 200 210 220 230 240 NANFYLQAGS AFAEMKIKGL LDRKGLWRSL NEMKRIFNFR RTPAAEHAFE HWQEDAFFAS 250 260 270 280 290 300 QFLNGLNPVL IRRCHYLPKN FPVTDAMVAS VLGPGTSLQA ELEKGSLFLV DHGILSGIQT 310 320 330 340 350 360 NVINGKPQFS AAPMTLLYQS PGCGPLLPLA IQLSQTPGPN SPIFLPTDDK WDWLLAKTWV 370 380 390 400 410 420 RNAEFSFHEA LTHLLHSHLL PEVFTLATLR QLPHCHPLFK STGIGIEGFS ELIQRNMKQL 430 440 450 460 470 480 NYSLLCLPED IRTRGVEDIP GYYYRDDGMQ IWGAVERFVS EIIGIYYPSD ESVQDDRELQ 490 500 510 520 530 540 AWVREIFSKG FLNQESSGIP SSLETREALV QYVTMVIFTC SAKHAAVSAG QFDSCAWMPN 550 560 570 580 590 600 LPPSMQLPPP TSKGLATCEG FIATLPPVNA TCDVILALWL LSKEPGDQRP LGTYPDEHFT 610 620 630 640 EEAPRRSIAT FQSRLAQISR GIQERNQGLV LPYTYLDPPL IENSVSI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Discovery of a second 15S-lipoxygenase in humans." Brash A.R., Boeglin W.E., Chang M.S. Proc. Natl. Acad. Sci. U.S.A. 94:6148-6152(1997) [PubMed: 9177185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT ARG-656. Tissue: Skin.
[2]	"A gene cluster encoding human epidermis-type lipoxygenases at chromosome 17p13.1: cloning, physical mapping, and expression." Krieg P., Marks F., Fuerstenberger G. Genomics 73:323-330(2001) [PubMed: 11350124] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-656.
[3]	"Evidence that arachidonate 15-lipoxygenase 2 is a negative cell cycle regulator in normal prostate epithelial cells." Tang S., Bhatia B., Maldonado C.J., Yang P., Newman R.A., Liu J., Chandra D., Traag J., Klein R.D., Fischer S.M., Chopra D., Shen J., Zhau H.E., Chung L.W.K., Tang D.G. J. Biol. Chem. 277:16189-16201(2002) [PubMed: 11839751] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C AND D), VARIANTS HIS-486 AND ARG-656.
[4]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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 A), VARIANT ARG-656. Tissue: Skin.
[7]	"Differential characteristics of human 15-lipoxygenase isozymes and a novel splice variant of 15S-lipoxygenase." Kilty I., Logan A., Vickers P.J. Eur. J. Biochem. 266:83-93(1999) [PubMed: 10542053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 337-484.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U78294 mRNA. Translation: AAB61706.1. AJ305028 , AJ305029, AJ305030, AJ305031 Genomic DNA. Translation: CAC34521.1. AF468051 mRNA. Translation: AAL76274.1. AF468052 mRNA. Translation: AAL76275.1. AF468053 mRNA. Translation: AAL76276.1. AF468054 mRNA. Translation: AAL76277.1. AC129492 Genomic DNA. No translation available. CH471108 Genomic DNA. Translation: EAW90098.1. CH471108 Genomic DNA. Translation: EAW90100.1. BC035217 mRNA. Translation: AAH35217.1. BC063647 mRNA. Translation: AAH63647.1. AF149095 Genomic DNA. Translation: AAD37786.1. Sequence problems.
IPI	IPI00005781. IPI00220009. IPI00220010. IPI00470667.
RefSeq	NP_001034219.1. NM_001039130.1. NP_001034220.1. NM_001039131.1. NP_001132.2. NM_001141.2.
UniGene	Hs.111256.
3D structure databases
ProteinModelPortal	O15296.
SMR	O15296. Positions 2-676.
ModBase	Search...
Protein-protein interaction databases
STRING	O15296.
Proteomic databases
PRIDE	O15296.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000380183; ENSP00000369530; ENSG00000179593.
GeneID	247.
KEGG	hsa:247.
UCSC	uc002gju.1. human. uc002gjv.1. human. uc002gjw.1. human.
Organism-specific databases
CTD	247.
GeneCards	GC17P007883.
H-InvDB	HIX0027139.
HGNC	HGNC:434. ALOX15B.
MIM	603697. gene.
neXtProt	NX_O15296.
PharmGKB	PA24725.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG13905.
GeneTree	ENSGT00550000074415.
HOVERGEN	HBG005150.
InParanoid	O15296.
OMA	ENYHEMF.
OrthoDB	EOG48SGSH.
PhylomeDB	O15296.
Gene expression databases
ArrayExpress	O15296.
Bgee	O15296.
CleanEx	HS_ALOX15B.
Genevestigator	O15296.
GermOnline	ENSG00000179593. Homo sapiens.
Family and domain databases
InterPro	IPR008976. Lipase_LipOase. IPR000907. LipOase. IPR013819. LipOase_C. IPR020834. LipOase_CS. IPR020833. LipOase_Fe_BS. IPR001024. LipOase_LH2. IPR001885. LipOase_mml. [Graphical view]
Gene3D	G3DSA:2.60.60.20. Lipase_LipOase. 1 hit.
KO	K08022.
PANTHER	PTHR11771. LipOase. 1 hit.
Pfam	PF00305. Lipoxygenase. 1 hit. PF01477. PLAT. 1 hit. [Graphical view]
PRINTS	PR00087. LIPOXYGENASE. PR00467. MAMLPOXGNASE.
SMART	SM00308. LH2. 1 hit. [Graphical view]
SUPFAM	SSF49723. Lipase_LipOase. 1 hit. SSF48484. Lipoxygenase. 1 hit.
PROSITE	PS00711. LIPOXYGENASE_1. 1 hit. PS00081. LIPOXYGENASE_2. 1 hit. PS51393. LIPOXYGENASE_3. 1 hit. PS50095. PLAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	985.
SOURCE	Search...

Entry information

Entry name

LX15B_HUMAN

Accession

Primary (citable) accession number: O15296
Secondary accession number(s): D3DTR2 , Q8IYQ2, Q8TEV3, Q8TEV4, Q8TEV5, Q8TEV6, Q9UKM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	January 11, 2011
Last modified:	December 14, 2011
This is version 116 of the entry and version 3 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.