ALOX15B

Functionⁱ

Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Converts arachidonic acid to 15S-hydroperoxyeicosatetraenoic acid/(15S)-HPETE. Also acts on linoleic acid to produce 13-hydroxyoctadecadienoic acid/13-HPODE. Has no detectable 8S-lipoxygenase activity but reacts with (8S)-HPETE to produce (8S,15S)-diHPETE. May regulate progression through the cell cycle and cell proliferation. May also regulate cytokine secretion by macrophages and therefore play a role in the immune response. May also regulate macrophage differentiation into proatherogenic foam cells.7 Publications

Caution

Despite its homology with mouse Alox8 (AC O35936), it seems not to have any 8S-lipoxygenase activity on arachidonate.Curated

Catalytic activityⁱ

Arachidonate + O₂ = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate.

Linoleate + O₂ = (9Z,11E)-13-hydroxyoctadeca-9,11-dienoate.

Cofactorⁱ

Fe cationPROSITE-ProRule annotation1 PublicationNote: Binds 1 Fe cation per subunit.PROSITE-ProRule annotation1 Publication

Kineticsⁱ

V_max=
4 µmol/min/mg enzyme with arachidonate as substrate (isoform A at pH 7.4 and 20 degrees Celsius)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 337-484, ALTERNATIVE SPLICING (ISOFORMS A AND D), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, KINETIC PARAMETERS, PATHWAY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
V_max=
2 µmol/min/mg enzyme with arachidonate as substrate (isoform D at pH 7.4 and 20 degrees Celsius)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 337-484, ALTERNATIVE SPLICING (ISOFORMS A AND D), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, KINETIC PARAMETERS, PATHWAY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
V_max=
4 µmol/min/mg enzyme with linoleate as substrate (isoform A at pH 7.4 and 20 degrees Celsius)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 337-484, ALTERNATIVE SPLICING (ISOFORMS A AND D), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, KINETIC PARAMETERS, PATHWAY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Pathwayⁱ: hydroperoxy eicosatetraenoic acid biosynthesis

This protein is involved in the pathway hydroperoxy eicosatetraenoic acid biosynthesis, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway hydroperoxy eicosatetraenoic acid biosynthesis and in Lipid metabolism.

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	15	Calcium 1; via carbonyl oxygen1 Publication	1
Metal bindingⁱ	17	Calcium 1; via carbonyl oxygen1 Publication	1
Metal bindingⁱ	39	Calcium 21 Publication	1
Metal bindingⁱ	40	Calcium 2; via carbonyl oxygen1 Publication	1
Metal bindingⁱ	42	Calcium 2; via carbonyl oxygen1 Publication	1
Metal bindingⁱ	44	Calcium 21 Publication	1
Metal bindingⁱ	85	Calcium 11 Publication	1
Metal bindingⁱ	86	Calcium 1; via carbonyl oxygen1 Publication	1
Metal bindingⁱ	373	Iron; catalyticPROSITE-ProRule annotation1 Publication	1
Metal bindingⁱ	378	Iron; catalyticPROSITE-ProRule annotation1 Publication	1
Metal bindingⁱ	553	Iron; catalyticPROSITE-ProRule annotation1 Publication	1
Metal bindingⁱ	676	Iron; via carboxylate; catalyticPROSITE-ProRule annotation1 Publication	1

GO - Molecular functionⁱ

arachidonate 15-lipoxygenase activity
Source: UniProtKB
Inferred from direct assayⁱ
arachidonate 8(S)-lipoxygenase activity Source: Ensembl
calcium ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 24497644
iron ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 24497644
linoleate 13S-lipoxygenase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 10542053
lipid binding Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

apoptotic process
Source: UniProtKB
Traceable author statementⁱ
- 11839751
arachidonic acid metabolic process
Source: UniProtKB
Inferred from direct assayⁱ
hepoxilin biosynthetic process Source: UniProtKB
linoleic acid metabolic process Source: Ensembl
lipid metabolic process
Source: UniProtKB
Traceable author statementⁱ
- 11839751
lipoxygenase pathway Source: Reactome
negative regulation of cell cycle
Source: UniProtKB
Inferred from direct assayⁱ
- 11839751
negative regulation of cell migration
Source: UniProtKB
Traceable author statementⁱ
- 11839751
negative regulation of cell proliferation
Source: UniProtKB
Inferred from direct assayⁱ
- 11839751
negative regulation of growth
Source: UniProtKB
Inferred from direct assayⁱ
- 11839751
positive regulation of chemokine secretion
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 18067895
positive regulation of keratinocyte differentiation Source: Ensembl
positive regulation of macrophage derived foam cell differentiation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 22912809
positive regulation of peroxisome proliferator activated receptor signaling pathway Source: Ensembl
prostate gland development
Source: UniProtKB
Non-traceable author statementⁱ
- 11839751
regulation of epithelial cell differentiation
Source: UniProtKB
Non-traceable author statementⁱ
- 11839751

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Dioxygenase, Oxidoreductase
Biological process	Lipid metabolism
Ligand	Calcium, Iron, Lipid-binding, Metal-binding

Enzyme and pathway databases

BRENDAⁱ	1.13.11.33 2681
Reactomeⁱ	R-HSA-2142770 Synthesis of 15-eicosatetraenoic acid derivatives
UniPathwayⁱ	UPA00881

Chemistry databases

SwissLipidsⁱ	SLP:000000651 SLP:000001469 [O15296-1] SLP:000001470 [O15296-4]

SwissLipidsⁱ

SLP:000000651
SLP:000001469 [O15296-1]
SLP:000001470 [O15296-4]

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Arachidonate 15-lipoxygenase B (EC:1.13.11.33) Short name: 15-LOX-B Alternative name(s): 15-lipoxygenase 2 Short name: 15-LOX-2 Arachidonate 15-lipoxygenase type II Linoleate 13-lipoxygenase 15-LOb (EC:1.13.11.-)
Gene namesⁱ	Name:ALOX15B
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 17

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000179593.15
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:434 ALOX15B
MIMⁱ	603697 gene
neXtProtⁱ	NX_O15296

Keywords - Cellular componentⁱ

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	39	D → A: Abolishes calcium-dependent association with membranes; when associated with A-44 and A-85. 1 Publication	1
Mutagenesisⁱ	44	E → A: Abolishes calcium-dependent association with membranes; when associated with A-39 and A-85. 1 Publication	1
Mutagenesisⁱ	85	D → A: Abolishes calcium-dependent association with membranes; when associated with A-39 and A-44. 1 Publication	1
Mutagenesisⁱ	602	D → Y: No effect on the stereoselectivity of the oxygenation reaction. Completely changes the stereoselectivity of the oxygenation reaction to produce (8S)-HPETE instead of (15S)-HPETE; when associated with H-603. 1 Publication	1
Mutagenesisⁱ	603	V → H: Changes the stereoselectivity of the oxygenation reaction. Completely changes the stereoselectivity of the oxygenation reaction to produce (8S)-HPETE instead of (15S)-HPETE; when associated with Y-602. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	247
Open Targets More...OpenTargetsⁱ	ENSG00000179593
PharmGKBⁱ	PA24725

Chemistry databases

ChEMBLⁱ	CHEMBL2457
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	1389

Polymorphism and mutation databases

BioMutaⁱ	ALOX15B

BioMutaⁱ

ALOX15B

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000220700	1 – 676	Arachidonate 15-lipoxygenase BAdd BLAST		676

Proteomic databases

EPDⁱ	O15296
PaxDbⁱ	O15296
PeptideAtlas More...PeptideAtlasⁱ	O15296
PRIDEⁱ	O15296
ProteomicsDBⁱ	48566 48567 [O15296-2] 48568 [O15296-3] 48569 [O15296-4]

PTM databases

iPTMnetⁱ	O15296
PhosphoSitePlusⁱ	O15296

Expressionⁱ

Tissue specificityⁱ

Expressed in hair, prostate, lung, ovary, lymph node, spinal cord and cornea.3 Publications

Inductionⁱ

Up-regulated by UV-irradiation.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000179593 Expressed in 107 organ(s), highest expression level in mammalian vulva
CleanExⁱ	HS_ALOX15B
ExpressionAtlasⁱ	O15296 baseline and differential
Genevisibleⁱ	O15296 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA010562

HPAⁱ

HPA010562

Interactionⁱ

Protein-protein interaction databases

BioGridⁱ	106748, 8 interactors
IntActⁱ	O15296, 5 interactors
STRINGⁱ	9606.ENSP00000369530

Chemistry databases

BindingDBⁱ

O15296

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	3 – 10	Combined sources	8
Beta strandⁱ	20 – 30	Combined sources	11
Beta strandⁱ	50 – 56	Combined sources	7
Beta strandⁱ	63 – 72	Combined sources	10
Turnⁱ	77 – 79	Combined sources	3
Beta strandⁱ	87 – 95	Combined sources	9
Beta strandⁱ	102 – 110	Combined sources	9
Beta strandⁱ	115 – 119	Combined sources	5
Turnⁱ	126 – 128	Combined sources	3
Helixⁱ	132 – 148	Combined sources	17
Beta strandⁱ	161 – 163	Combined sources	3
Helixⁱ	167 – 169	Combined sources	3
Helixⁱ	172 – 174	Combined sources	3
Helixⁱ	178 – 197	Combined sources	20
Helixⁱ	212 – 215	Combined sources	4
Helixⁱ	216 – 219	Combined sources	4
Helixⁱ	223 – 231	Combined sources	9
Helixⁱ	235 – 244	Combined sources	10
Helixⁱ	265 – 272	Combined sources	8
Helixⁱ	278 – 284	Combined sources	7
Beta strandⁱ	287 – 291	Combined sources	5
Helixⁱ	293 – 295	Combined sources	3
Beta strandⁱ	314 – 319	Combined sources	6
Turnⁱ	321 – 323	Combined sources	3
Beta strandⁱ	326 – 336	Combined sources	11
Helixⁱ	350 – 370	Combined sources	21
Turnⁱ	371 – 373	Combined sources	3
Helixⁱ	374 – 377	Combined sources	4
Helixⁱ	379 – 391	Combined sources	13
Helixⁱ	397 – 402	Combined sources	6
Helixⁱ	403 – 406	Combined sources	4
Helixⁱ	409 – 419	Combined sources	11
Helixⁱ	426 – 430	Combined sources	5
Helixⁱ	434 – 446	Combined sources	13
Helixⁱ	451 – 454	Combined sources	4
Helixⁱ	456 – 462	Combined sources	7
Helixⁱ	472 – 495	Combined sources	24
Helixⁱ	499 – 503	Combined sources	5
Helixⁱ	506 – 518	Combined sources	13
Turnⁱ	519 – 522	Combined sources	4
Helixⁱ	524 – 526	Combined sources	3
Helixⁱ	535 – 549	Combined sources	15
Helixⁱ	551 – 557	Combined sources	7
Helixⁱ	560 – 564	Combined sources	5
Helixⁱ	567 – 569	Combined sources	3
Beta strandⁱ	574 – 576	Combined sources	3
Beta strandⁱ	580 – 583	Combined sources	4
Helixⁱ	587 – 593	Combined sources	7
Helixⁱ	597 – 611	Combined sources	15
Helixⁱ	631 – 656	Combined sources	26
Helixⁱ	667 – 669	Combined sources	3
Beta strandⁱ	670 – 673	Combined sources	4

Show more details

3D structure databases

ProteinModelPortalⁱ	O15296
SMRⁱ	O15296
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	2 – 124	PLATPROSITE-ProRule annotationAdd BLAST		123
Domainⁱ	125 – 676	LipoxygenasePROSITE-ProRule annotationAdd BLAST		552

Domainⁱ

The PLAT domain can bind calcium ions; this promotes association with membranes.

Sequence similaritiesⁱ

Belongs to the lipoxygenase family.Curated

Phylogenomic databases

eggNOGⁱ	ENOG410IF0U Eukaryota ENOG410YN4N LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00550000074415
HOVERGENⁱ	HBG005150
InParanoidⁱ	O15296
KEGG Orthology (KO) More...KOⁱ	K08022
OMAⁱ	EFSIHEA
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G04A4
PhylomeDBⁱ	O15296
TreeFamⁱ	TF105320

Family and domain databases

InterProⁱ	View protein in InterPro IPR000907 LipOase IPR013819 LipOase_C IPR036226 LipOase_C_sf IPR020834 LipOase_CS IPR020833 LipOase_Fe_BS IPR001885 LipOase_mml IPR001024 PLAT/LH2_dom IPR036392 PLAT/LH2_dom_sf
PANTHERⁱ	PTHR11771 PTHR11771, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00305 Lipoxygenase, 1 hit PF01477 PLAT, 1 hit
PRINTSⁱ	PR00087 LIPOXYGENASE PR00467 MAMLPOXGNASE
SMARTⁱ	View protein in SMART SM00308 LH2, 1 hit
SUPFAMⁱ	SSF48484 SSF48484, 1 hit SSF49723 SSF49723, 1 hit
PROSITEⁱ	View protein in PROSITE PS00711 LIPOXYGENASE_1, 1 hit PS00081 LIPOXYGENASE_2, 1 hit PS51393 LIPOXYGENASE_3, 1 hit PS50095 PLAT, 1 hit

Sequences (4+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 4 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show all Align All

Isoform A (identifier: O15296-1) [UniParc]FASTA Add to basket

Also known as: 15-LOb1

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.

« Hide

        10         20         30         40         50
MAEFRVRVST GEAFGAGTWD KVSVSIVGTR GESPPLPLDN LGKEFTAGAE 
        60         70         80         90        100
EDFQVTLPED VGRVLLLRVH KAPPVLPLLG PLAPDAWFCR WFQLTPPRGG 
       110        120        130        140        150
HLLFPCYQWL EGAGTLVLQE GTAKVSWADH HPVLQQQRQE ELQARQEMYQ 
       160        170        180        190        200
WKAYNPGWPH CLDEKTVEDL ELNIKYSTAK NANFYLQAGS AFAEMKIKGL 
       210        220        230        240        250
LDRKGLWRSL NEMKRIFNFR RTPAAEHAFE HWQEDAFFAS QFLNGLNPVL 
       260        270        280        290        300
IRRCHYLPKN FPVTDAMVAS VLGPGTSLQA ELEKGSLFLV DHGILSGIQT 
       310        320        330        340        350
NVINGKPQFS AAPMTLLYQS PGCGPLLPLA IQLSQTPGPN SPIFLPTDDK 
       360        370        380        390        400
WDWLLAKTWV RNAEFSFHEA LTHLLHSHLL PEVFTLATLR QLPHCHPLFK 
       410        420        430        440        450
LLIPHTRYTL HINTLARELL IVPGQVVDRS TGIGIEGFSE LIQRNMKQLN 
       460        470        480        490        500
YSLLCLPEDI RTRGVEDIPG YYYRDDGMQI WGAVERFVSE IIGIYYPSDE 
       510        520        530        540        550
SVQDDRELQA WVREIFSKGF LNQESSGIPS SLETREALVQ YVTMVIFTCS 
       560        570        580        590        600
AKHAAVSAGQ FDSCAWMPNL PPSMQLPPPT SKGLATCEGF IATLPPVNAT 
       610        620        630        640        650
CDVILALWLL SKEPGDQRPL GTYPDEHFTE EAPRRSIATF QSRLAQISRG 
       660        670 
IQERNQGLVL PYTYLDPPLI ENSVSI

Length:676

Mass (Da):75,857

Last modified:January 11, 2011 - v3

Checksum:ⁱ4F641DF2F9D492C6

GO

Isoform B (identifier: O15296-2) [UniParc]FASTA Add to basket

Also known as: 15-LOX2sv-b

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

« Hide

        10         20         30         40         50
MAEFRVRVST GEAFGAGTWD KVSVSIVGTR GESPPLPLDN LGKEFTAGAE 
        60         70         80         90        100
EDFQVTLPED VGRVLLLRVH KAPPVLPLLG PLAPDAWFCR WFQLTPPRGG 
       110        120        130        140        150
HLLFPCYQWL EGAGTLVLQE GTAKVSWADH HPVLQQQRQE ELQARQEMYQ 
       160        170        180        190        200
WKAYNPGWPH CLDEKTVEDL ELNIKYSTAK NANFYLQAGS AFAEMKIKGL 
       210        220        230        240        250
LDRKGLWRSL NEMKRIFNFR RTPAAEHAFE HWQEDAFFAS QFLNGLNPVL 
       260        270        280        290        300
IRRCHYLPKN FPVTDAMVAS VLGPGTSLQA ELEKGSLFLV DHGILSGIQT 
       310        320        330        340        350
NVINGKPQFS AAPMTLLYQS PGCGPLLPLA IQLSQTPGPN SPIFLPTDDK 
       360        370        380        390        400
WDWLLAKTWV RNAEFSFHEA LTHLLHSHLL PEVFTLATLR QLPHCHPLFK 
       410        420        430        440        450
STGIGIEGFS ELIQRNMKQL NYSLLCLPED IRTRGVEDIP GYYYRDDGMQ 
       460        470        480        490        500
IWGIPSSLET REALVQYVTM VIFTCSAKHA AVSAGQFDSC AWMPNLPPSM 
       510        520        530        540        550
QLPPPTSKGL ATCEGFIATL PPVNATCDVI LALWLLSKEP GDQRPLGTYP 
       560        570        580        590        600
DEHFTEEAPR RSIATFQSRL AQISRGIQER NQGLVLPYTY LDPPLIENSV 

SI

Show »

Length:602

Mass (Da):67,345

Checksum:ⁱ8804BB44095695C2

GO

Isoform C (identifier: O15296-3) [UniParc]FASTA Add to basket

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.

« Hide

        10         20         30         40         50
MAEFRVRVST GEAFGAGTWD KVSVSIVGTR GESPPLPLDN LGKEFTAGAE 
        60         70         80         90        100
EDFQVTLPED VGRVLLLRVH KAPPVLPLLG PLAPDAWFCR WFQLTPPRGG 
       110        120        130        140        150
HLLFPCYQWL EGAGTLVLQE GTAKVSWADH HPVLQQQRQE ELQARQEMYQ 
       160        170        180        190        200
WKAYNPGWPH CLDEKTVEDL ELNIKYSTAK NANFYLQAGS AFAEMKIKGL 
       210        220        230        240        250
LDRKGLWRSL NEMKRIFNFR RTPAAEHAFE HWQEDAFFAS QFLNGLNPVL 
       260        270        280        290        300
IRRCHYLPKN FPVTDAMVAS VLGPGTSLQA ELEKGSLFLV DHGILSGIQT 
       310        320        330        340        350
NVINGKPQFS AAPMTLLYQS PGCGPLLPLA IQLSQTPGPN SPIFLPTDDK 
       360        370        380        390        400
WDWLLAKTWV RNAEFSFHEA LTHLLHSHLL PEVFTLATLR QLPHCHPLFK 
       410        420        430        440        450
LLIPHTRYTL HINTLARELL IVPGQVVDRS TGIGIEGFSE LIQRNMKQLN 
       460        470        480        490        500
YSLLCLPEDI RTRGVEDIPG YYYRDDGMQI WGAVERFVSE IIGIYYPSDE 
       510        520        530        540        550
SVQDDRELQA WVREIFSKGF LNQESSGIPS SLETREALVQ YVTMVIFTCS 
       560        570        580        590        600
AKHAAVSAGQ VRKGQRPRWQ AGGDPAPQPH SALSAFSLTP VLGCPTCHPA 
       610 
CSCHHPPPKA WQHARAS

Show »

Length:617

Mass (Da):69,136

Checksum:ⁱ3F690488B2B766AC

GO

Isoform D (identifier: O15296-4) [UniParc]FASTA Add to basket

Also known as: 15-LOX2sv-a, 15-LOb2

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

« Hide

        10         20         30         40         50
MAEFRVRVST GEAFGAGTWD KVSVSIVGTR GESPPLPLDN LGKEFTAGAE 
        60         70         80         90        100
EDFQVTLPED VGRVLLLRVH KAPPVLPLLG PLAPDAWFCR WFQLTPPRGG 
       110        120        130        140        150
HLLFPCYQWL EGAGTLVLQE GTAKVSWADH HPVLQQQRQE ELQARQEMYQ 
       160        170        180        190        200
WKAYNPGWPH CLDEKTVEDL ELNIKYSTAK NANFYLQAGS AFAEMKIKGL 
       210        220        230        240        250
LDRKGLWRSL NEMKRIFNFR RTPAAEHAFE HWQEDAFFAS QFLNGLNPVL 
       260        270        280        290        300
IRRCHYLPKN FPVTDAMVAS VLGPGTSLQA ELEKGSLFLV DHGILSGIQT 
       310        320        330        340        350
NVINGKPQFS AAPMTLLYQS PGCGPLLPLA IQLSQTPGPN SPIFLPTDDK 
       360        370        380        390        400
WDWLLAKTWV RNAEFSFHEA LTHLLHSHLL PEVFTLATLR QLPHCHPLFK 
       410        420        430        440        450
STGIGIEGFS ELIQRNMKQL NYSLLCLPED IRTRGVEDIP GYYYRDDGMQ 
       460        470        480        490        500
IWGAVERFVS EIIGIYYPSD ESVQDDRELQ AWVREIFSKG FLNQESSGIP 
       510        520        530        540        550
SSLETREALV QYVTMVIFTC SAKHAAVSAG QFDSCAWMPN LPPSMQLPPP 
       560        570        580        590        600
TSKGLATCEG FIATLPPVNA TCDVILALWL LSKEPGDQRP LGTYPDEHFT 
       610        620        630        640 
EEAPRRSIAT FQSRLAQISR GIQERNQGLV LPYTYLDPPL IENSVSI

Show »

Length:647

Mass (Da):72,523

Checksum:ⁱEE51EEA9221CCC4B

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	I3L1D5	I3L1D5_HUMAN		Arachidonate 15-lipoxygenase B Arachidonate 15-lipoxygenase B	ALOX15B	664	Annotation score:

Sequence cautionⁱ

The sequence AAD37786 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	271	V → L in AAB61706 (PubMed:9177185).Curated	1
Sequence conflictⁱ	271	V → L in CAC34521 (PubMed:11350124).Curated	1
Sequence conflictⁱ	338	G → C in AAD37786 (PubMed:15489334).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_061334	486	R → H1 PublicationCorresponds to variant dbSNP:rs9895916Ensembl.	1
Natural variantⁱVAR_024524	656	Q → R4 PublicationsCorresponds to variant dbSNP:rs4792147Ensembl.	1
Natural variantⁱVAR_024525	676	I → V. Corresponds to variant dbSNP:rs7225107Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_003142	401 – 429	Missing in isoform B and isoform D. 1 PublicationAdd BLAST	29
Alternative sequenceⁱVSP_003143	483 – 527	Missing in isoform B. 1 PublicationAdd BLAST	45
Alternative sequenceⁱVSP_003144	561 – 617	FDSCA…EPGDQ → VRKGQRPRWQAGGDPAPQPH SALSAFSLTPVLGCPTCHPA CSCHHPPPKAWQHARAS in isoform C. 1 PublicationAdd BLAST	57
Alternative sequenceⁱVSP_003145	618 – 676	Missing in isoform C. 1 PublicationAdd BLAST	59

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS11128.1 [O15296-1] CCDS32558.1 [O15296-4] CCDS32559.1 [O15296-2]
NCBI Reference Sequences More...RefSeqⁱ	NP_001034219.1, NM_001039130.1 [O15296-4] NP_001034220.1, NM_001039131.1 [O15296-2] NP_001132.2, NM_001141.2 [O15296-1]
UniGeneⁱ	Hs.111256

Genome annotation databases

Ensemblⁱ	ENST00000380173; ENSP00000369520; ENSG00000179593 [O15296-4] ENST00000380183; ENSP00000369530; ENSG00000179593 [O15296-1] ENST00000573359; ENSP00000460332; ENSG00000179593 [O15296-2]
GeneIDⁱ	247
KEGGⁱ	hsa:247
UCSC genome browser More...UCSCⁱ	uc002gju.4 human [O15296-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
O15296	Uncharacterized protein		AOTNA		677	UniRef90_O15296
Arachidonate 15-lipoxygenase B		MACMU		676
ALOX15B isoform 2		PONAB		676
Uncharacterized protein		RHIRO		676
Uncharacterized protein		MANLE		676
+30
O15296-2	Uncharacterized protein		MACMU		621	UniRef90_O15296-2
Uncharacterized protein		COLAP		602
ALOX15B isoform 5		PONAB		602
ALOX15B isoform 5		PANTR		602
Uncharacterized protein		CERAT		602
+11
O15296-4	Uncharacterized protein		COLAP		647	UniRef90_O15296-4
ALOX15B isoform 3		PONAB		647
ALOX15B isoform 3		PANTR		647
Uncharacterized protein		CERAT		647
Uncharacterized protein		RHIRO		647
+9

Protein	Similar proteins		Species	Score	Length	Source
O15296	Arachidonate 15-lipoxygenase B		RAT		677	UniRef50_O15296
Arachidonate 8S-lipoxygenase		MOUSE		677
Uncharacterized protein		AOTNA		677
Uncharacterized protein		COLAP		676
Uncharacterized protein		RHIBE		676
+193

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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.
CCDSⁱ	CCDS11128.1 [O15296-1] CCDS32558.1 [O15296-4] CCDS32559.1 [O15296-2]
RefSeqⁱ	NP_001034219.1, NM_001039130.1 [O15296-4] NP_001034220.1, NM_001039131.1 [O15296-2] NP_001132.2, NM_001141.2 [O15296-1]
UniGeneⁱ	Hs.111256

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4NRE	X-ray	2.63	A	1-676	[»]
ProteinModelPortalⁱ	O15296
SMRⁱ	O15296
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	106748, 8 interactors
IntActⁱ	O15296, 5 interactors
STRINGⁱ	9606.ENSP00000369530

Chemistry databases

BindingDBⁱ	O15296
ChEMBLⁱ	CHEMBL2457
GuidetoPHARMACOLOGYⁱ	1389
SwissLipidsⁱ	SLP:000000651 SLP:000001469 [O15296-1] SLP:000001470 [O15296-4]

PTM databases

iPTMnetⁱ	O15296
PhosphoSitePlusⁱ	O15296

Polymorphism and mutation databases

BioMutaⁱ	ALOX15B

BioMutaⁱ

ALOX15B

Proteomic databases

EPDⁱ	O15296
PaxDbⁱ	O15296
PeptideAtlasⁱ	O15296
PRIDEⁱ	O15296
ProteomicsDBⁱ	48566 48567 [O15296-2] 48568 [O15296-3] 48569 [O15296-4]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	247
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000380173; ENSP00000369520; ENSG00000179593 [O15296-4] ENST00000380183; ENSP00000369530; ENSG00000179593 [O15296-1] ENST00000573359; ENSP00000460332; ENSG00000179593 [O15296-2]
GeneIDⁱ	247
KEGGⁱ	hsa:247
UCSCⁱ	uc002gju.4 human [O15296-1]

Organism-specific databases

CTDⁱ	247
DisGeNETⁱ	247
EuPathDBⁱ	HostDB:ENSG00000179593.15
GeneCardsⁱ	ALOX15B
H-InvDBⁱ	HIX0027139
HGNCⁱ	HGNC:434 ALOX15B
HPAⁱ	HPA010562
MIMⁱ	603697 gene
neXtProtⁱ	NX_O15296
OpenTargetsⁱ	ENSG00000179593
PharmGKBⁱ	PA24725
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	ENOG410IF0U Eukaryota ENOG410YN4N LUCA
GeneTreeⁱ	ENSGT00550000074415
HOVERGENⁱ	HBG005150
InParanoidⁱ	O15296
KOⁱ	K08022
OMAⁱ	EFSIHEA
OrthoDBⁱ	EOG091G04A4
PhylomeDBⁱ	O15296
TreeFamⁱ	TF105320

Enzyme and pathway databases

UniPathwayⁱ	UPA00881
BRENDAⁱ	1.13.11.33 2681
Reactomeⁱ	R-HSA-2142770 Synthesis of 15-eicosatetraenoic acid derivatives

Miscellaneous databases

ChiTaRSⁱ	ALOX15B human
GeneWikiⁱ	ALOX15B
GenomeRNAiⁱ	247
Protein Ontology More...PROⁱ	PR:O15296
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000179593 Expressed in 107 organ(s), highest expression level in mammalian vulva
CleanExⁱ	HS_ALOX15B
ExpressionAtlasⁱ	O15296 baseline and differential
Genevisibleⁱ	O15296 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR000907 LipOase IPR013819 LipOase_C IPR036226 LipOase_C_sf IPR020834 LipOase_CS IPR020833 LipOase_Fe_BS IPR001885 LipOase_mml IPR001024 PLAT/LH2_dom IPR036392 PLAT/LH2_dom_sf
PANTHERⁱ	PTHR11771 PTHR11771, 1 hit
Pfamⁱ	View protein in Pfam PF00305 Lipoxygenase, 1 hit PF01477 PLAT, 1 hit
PRINTSⁱ	PR00087 LIPOXYGENASE PR00467 MAMLPOXGNASE
SMARTⁱ	View protein in SMART SM00308 LH2, 1 hit
SUPFAMⁱ	SSF48484 SSF48484, 1 hit SSF49723 SSF49723, 1 hit
PROSITEⁱ	View protein in PROSITE PS00711 LIPOXYGENASE_1, 1 hit PS00081 LIPOXYGENASE_2, 1 hit PS51393 LIPOXYGENASE_3, 1 hit PS50095 PLAT, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	LX15B_HUMAN
Accessionⁱ	O15296Primary (citable) accession number: O15296 Secondary accession number(s): D3DTR2 Q9UKM4
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
	Last sequence update:	January 11, 2011
	Last modified:	November 7, 2018
	This is version 175 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PATHWAY comments
Index of metabolic and biosynthesis pathways
Human chromosome 17
Human chromosome 17: entries, gene names and cross-references to MIM
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

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UniProtKB - O15296 (LX15B_HUMAN)

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Arachidonate 15-lipoxygenase B

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Caution

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: hydroperoxy eicosatetraenoic acid biosynthesis

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GO - Biological processi

Enzyme and pathway databases

Chemistry databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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Extracellular region or secreted

Nucleus

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Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

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Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

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<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

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<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

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Protein-protein interaction databases

Chemistry databases

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Protocols and materials databases

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Functionⁱ

Kineticsⁱ

Pathwayⁱ: hydroperoxy eicosatetraenoic acid biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ