SMART: Pfam domain Lamp

The domain within your query sequence starts at position 26 and ends at position 268; the E-value for the Lamp domain shown below is 8.3e-26.

QTVAEQEVENLSGLSTNPEKDIFVVRENGTTCLMAEFAAKFIVPYDVWASNYVDLITEQA
EISLTRGAEVKGHCGHNESELEVFWVDHAYTLRMLFVKESHNTSKGPEATWNLNKVHFVY
DSSEKTHFKAPVKVNKYIASSHHLSALVTPAGMSYECQAQQTISLASSDPQKTVTMILSA
VHIQPFDIISDFVFSEEHKCPVDEQEQLEETLPLILGLILGLVIVITLVIYHIHHKMTAN
QVQ

Lamp

PFAM accession number:	PF01299
Interpro abstract (IPR002000):	Lysosome-associated membrane glycoproteins (lamp) [ (PUBMED:1939168) ] are integral membrane proteins, specific to lysosomes, and whose exact biological function is not yet clear. Structurally, the lamp proteins consist of two internally homologous lysosome-luminal domains separated by a proline-rich hinge region; at the C-terminal extremity there is a transmembrane region (TM) followed by a very short cytoplasmic tail (C). In each of the duplicated domains, there are two conserved disulphide bonds. This structure is schematically represented in the figure below. +-----+ +-----+ +-----+ +-----+ \| \| \| \| \| \| \| \| xCxxxxxCxxxxxxxxxxxxCxxxxxCxxxxxxxxxCxxxxxCxxxxxxxxxxxxCxxxxxCxxxxxxxx +--------------------------++Hinge++--------------------------++TM++C+ In mammals, there are two closely related types of lamp: lamp-1 and lamp-2, which form major components of the lysosome membrane. In chicken lamp-1 is known as LEP100. Also included in this entry is the macrophage protein CD68 (or macrosialin) [ (PUBMED:8486654) ] is a heavily glycosylated integral membrane protein whose structure consists of a mucin-like domain followed by a proline-rich hinge; a single lamp-like domain; a transmembrane region and a short cytoplasmic tail. Similar to CD68, mammalian lamp-3, which is expressed in lymphoid organs, dendritic cells and in lung, contains all the C-terminal regions but lacks the N-terminal lamp-like region [ (PUBMED:9768752) ]. In a lamp-family protein from nematodes [ (PUBMED:10862717) ] only the part C-terminal to the hinge is conserved.
GO component:	membrane (GO:0016020)

PFAM accession number:

PF01299

Interpro abstract (IPR002000):

Lysosome-associated membrane glycoproteins (lamp) [ (PUBMED:1939168) ] are integral membrane proteins, specific to lysosomes, and whose exact biological function is not yet clear. Structurally, the lamp proteins consist of two internally homologous lysosome-luminal domains separated by a proline-rich hinge region; at the C-terminal extremity there is a transmembrane region (TM) followed by a very short cytoplasmic tail (C). In each of the duplicated domains, there are two conserved disulphide bonds. This structure is schematically represented in the figure below.


   +-----+            +-----+         +-----+            +-----+
   |     |            |     |         |     |            |     |
  xCxxxxxCxxxxxxxxxxxxCxxxxxCxxxxxxxxxCxxxxxCxxxxxxxxxxxxCxxxxxCxxxxxxxx
  +--------------------------++Hinge++--------------------------++TM++C+

In mammals, there are two closely related types of lamp: lamp-1 and lamp-2, which form major components of the lysosome membrane. In chicken lamp-1 is known as LEP100.

Also included in this entry is the macrophage protein CD68 (or macrosialin) [ (PUBMED:8486654) ] is a heavily glycosylated integral membrane protein whose structure consists of a mucin-like domain followed by a proline-rich hinge; a single lamp-like domain; a transmembrane region and a short cytoplasmic tail.

Similar to CD68, mammalian lamp-3, which is expressed in lymphoid organs, dendritic cells and in lung, contains all the C-terminal regions but lacks the N-terminal lamp-like region [ (PUBMED:9768752) ]. In a lamp-family protein from nematodes [ (PUBMED:10862717) ] only the part C-terminal to the hinge is conserved.

GO component:

membrane (GO:0016020)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Lamp