The domain within your query sequence starts at position 2 and ends at position 112; the E-value for the LH2 domain shown below is 2.18e-37.

GVYRIRVSTGDSVYAGSNNEVYLWLIGQHGEASLGKLFRPCRNSEAEFKVDVSEYLGPLL
FVRVQKWHYLKEDAWFCNWISVKGPGDQGSEYTFPCYRWVQGTSILNLPEG

LH2

Lipoxygenase homology 2 (beta barrel) domain

• SMART accession number: SM00308
• Description: -
• Interpro abstract (IPR001024):

  This entry represents a domain found in a variety of membrane or lipid associated proteins. It is known as the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain, is found in a variety of membrane or lipid associated proteins. Structurally, this domain forms a beta-sandwich composed of two sheets of four strands each [ (PUBMED:10469604) (PUBMED:11985859) (PUBMED:11412104) ]. The most highly conserved regions coincide with the beta-strands, with most of the highly conserved residues being buried within the protein. An exception to this is a surface lysine or arginine that occurs on the surface of the fifth beta-strand of the eukaryotic domains. In pancreatic lipase, the lysine in this position forms a salt bridge with the procolipase protein. The conservation of a charged surface residue may indicate the location of a conserved ligand-binding site. It is thought that this domain may mediate membrane attachment via other protein binding partners.

• GO function: protein binding (GO:0005515)

There are 13940 LH2 domains in 7296 proteins in SMART's nrdb database.

Literature (relevant references for this domain)

Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

• Aravind L, Ponting CP
• The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins.
• FEMS Microbiol Lett. 1999; 176: 111-6

Mutations in the cytoplasmic linker regions of receptor histidine kinase and chemoreceptor proteins have been shown previously to significantly impair receptor functions. Here we demonstrate significant sequence similarities between these regions in numerous histidine kinases, methyl-accepting proteins, adenylyl cyclases and other prokaryotic signalling proteins. It is suggested that these 'HAMP domains' possess roles of regulating the phosphorylation or methylation of homodimeric receptors by transmitting the conformational changes in periplasmic ligand-binding domains to cytoplasmic signalling kinase and methyl-acceptor domains.

• Bateman A, Sandford R
• The PLAT domain: a new piece in the PKD1 puzzle.
• Curr Biol. 1999; 9: 58890-58890

• Ponting CP, Hofmann K, Bork P
• A latrophilin/CL-1-like GPS domain in polycystin-1.
• Curr Biol. 1999; 9: 5858-5858

Disease (disease genes where sequence variants are found in this domain)

SwissProt sequences and OMIM curated human diseases associated with missense mutations within the LH2 domain.

Protein	Disease
Lipoprotein lipase (P06858) (SMART)	OMIM:238600: Hyperlipoproteinemia I ; Lipoprotein lipase deficiency ; Chylomicronemia syndrome, familial ; Combined hyperlipemia, familial
Hepatic triacylglycerol lipase (P11150) (SMART)	OMIM:151670: Hepatic lipase deficiency

Metabolism (metabolic pathways involving proteins which contain this domain)

% proteins involved	KEGG pathway ID	Description
29.91	map00590	Arachidonic acid metabolism
27.10	map00561	Glycerolipid metabolism
15.89	map00591	Linoleic acid metabolism
7.48	map05010	Alzheimer's disease
7.48	map03320	PPAR signaling pathway
5.61	map00592	alpha-Linolenic acid metabolism
0.93	map00628	Fluorene degradation
0.93	map00380	Tryptophan metabolism
0.93	map00626	Naphthalene and anthracene degradation
0.93	map00643	Styrene degradation
0.93	map00362	Benzoate degradation via hydroxylation
0.93	map00351	1,1,1-Trichloro-2,2-bis(4-chlorophenyl)ethane (DDT) degradation
0.93	map00623	2,4-Dichlorobenzoate degradation

This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with LH2 domain which could be assigned to a KEGG orthologous group, and not all proteins containing LH2 domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

Structure (3D structures containing this domain)

3D Structures of LH2 domains in PDB

PDB code	Title
1bu8	RAT PANCREATIC LIPASE RELATED PROTEIN 2
1eth	TRIACYLGLYCEROL LIPASE/COLIPASE COMPLEX
1f8n	LIPOXYGENASE-1 (SOYBEAN) AT 100K, NEW REFINEMENT
1fgm	LIPOXYGENASE-1 (SOYBEAN) AT 100K, N694H MUTANT
1fgo	LIPOXYGENASE-1 (SOYBEAN) AT 100K, Q495A MUTANT
1fgq	LIPOXYGENASE-1 (SOYBEAN) AT 100K, Q495E MUTANT
1fgr	LIPOXYGENASE-1 (SOYBEAN) AT 100K, Q697E MUTANT
1fgt	LIPOXYGENASE-1 (SOYBEAN) AT 100K, Q697N MUTANT
1gpl	RP2 LIPASE
1hpl	HORSE PANCREATIC LIPASE. THE CRYSTAL STRUCTURE AT 2.3 ANGSTROMS RESOLUTION
1hu9	LIPOXYGENASE-3 (SOYBEAN) COMPLEX WITH 4-HYDROPEROXY-2-METHOXY-PHENOL
1ik3	LIPOXYGENASE-3 (SOYBEAN) COMPLEX WITH 13(S)-HYDROPEROXY-9(Z),11(E)-OCTADECADIENOIC ACID
1jnq	LIPOXYGENASE-3 (SOYBEAN) COMPLEX WITH EPIGALLOCATHECHIN (EGC)
1lnh	LIPOXYGENASE-3(SOYBEAN) NON-HEME FE(II) METALLOPROTEIN
1lox	RABBIT RETICULOCYTE 15-LIPOXYGENASE
1lpa	INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE COMPLEX BY MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY
1lpb	THE 2.46 ANGSTROMS RESOLUTION STRUCTURE OF THE PANCREATIC LIPASE COLIPASE COMPLEX INHIBITED BY A C11 ALKYL PHOSPHONATE
1n8q	LIPOXYGENASE IN COMPLEX WITH PROTOCATECHUIC ACID
1n8s	Structure of the pancreatic lipase-colipase complex
1no3	REFINED STRUCTURE OF SOYBEAN LIPOXYGENASE-3 WITH 4-NITROCATECHOL AT 2.15 ANGSTROM RESOLUTION
1rov	Lipoxygenase-3 Treated with Cumene Hydroperoxide
1rp1	DOG PANCREATIC LIPASE RELATED PROTEIN 1
1rrh	Soybean Lipoxygenase (LOX-3) at ambient temperatures at 2.0 A resolution
1rrl	Soybean Lipoxygenase (LOX-3) at 93K at 2.0 A resolution
1w52	Crystal structure of a proteolyzed form of pancreatic lipase related protein 2 from horse
1y4k	Lipoxygenase-1 (Soybean) at 100K, N694G Mutant
1yge	LIPOXYGENASE-1 (SOYBEAN) AT 100K
2fnq	Insights from the X-ray crystal structure of coral 8R-lipoxygenase: calcium activation via A C2-like domain and a structural basis of product chirality
2iuj	Crystal Structure of Soybean Lipoxygenase-B
2iuk	Crystal structure of Soybean Lipoxygenase-D
2oxe	Structure of the Human Pancreatic Lipase-related Protein 2
2p0m	Revised structure of rabbit reticulocyte 15S-lipoxygenase
2ppl	Human Pancreatic lipase-related protein 1
2pvs	Structure of human pancreatic lipase related protein 2 mutant N336Q
2sbl	THE THREE-DIMENSIONAL STRUCTURE OF AN ARACHIDONIC ACID 15-LIPOXYGENASE
3bnb	Lipoxygenase-1 (Soybean) I553L Mutant
3bnc	Lipoxygenase-1 (Soybean) I553G Mutant
3bnd	Lipoxygenase-1 (Soybean), I553V Mutant
3bne	Lipoxygenase-1 (Soybean) I553A Mutant
3dy5	Allene oxide synthase 8R-lipoxygenase from Plexaura homomalla
3fg1	Crystal structure of Delta413-417:GS LOX
3fg3	Crystal structure of Delta413-417:GS I805W LOX
3fg4	Crystal structure of Delta413-417:GS I805A LOX
3o8y	Stable-5-Lipoxygenase
3pzw	Soybean lipoxygenase-1 - re-refinement
3v92	S663A Stable-5-LOX
3v98	S663D Stable-5-LOX
3v99	S663D Stable-5-LOX in complex with Arachidonic Acid
3vf1	Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca-regulation
4nre	The structure of human 15-lipoxygenase-2 with a substrate mimic
4qwt	4QWT
4wfo	4WFO
4wha	4WHA
5eeo	5EEO

Links (links to other resources describing this domain)

• INTERPRO: IPR001024
• PFAM: lipoxygenase
• PROSITE: LIPOXYGENASE_1