attractin (Mahogany homolog, DPPT-L, ATRN, KIAA0548, MGCA)

Function: 1) initial immune cell clustering during inflammatory response 2) regulates chemotactic activity of chemokines (putative) 3) activation of peripheral blood leukocytes with phytohemagglutinin induces strong expression of membrane isoform followed by the release of secreted isoform 4) melanocortin signaling pathways that regulate energy homeostasis & hair color (putative) 5) low-affinity receptor for agouti (putative) 6) myelination in the central nervous system Structure: - contains 1 C-type lectin domain. - contains 1 CUB domain. - contains 1 EGF-like domain. - contains 6 Kelch repeats. - contains 2 laminin EGF-like domains Compartment: - isoform 1: cell membrane - isoforms 2,3,4,5: secreted Alternative splicing: named isoforms=3 Expression: - expressed & secreted by activated T lymphocytes - expressed at low to moderate levels in peripheral blood leukocytes, spleen, lymph node, tonsil, bone marrow, fetal liver - very low levels found in thymus - isoform 2 (secreted) is the major isoform in peripheral blood leukocytes

General

glycoprotein membrane protein secreted protein

Properties

SIZE: MW = 159 kD entity length = 1429 aa COMPARTMENT: cellular membrane MOTIF: signal sequence {1-15} alanine-rich region {81-89} MOTIF: alanine residue (SEVERAL) EGF domain {101-129} MOTIF: cysteine residue {C101} MODIFICATION: cysteine residue {C111} cysteine residue {C105} MODIFICATION: cysteine residue {C118} cysteine residue {C111} MODIFICATION: cysteine residue {C101} cysteine residue {C118} MODIFICATION: cysteine residue {C105} cysteine residue {C120} MODIFICATION: cysteine residue {C129} cysteine residue {C129} MODIFICATION: cysteine residue {C120} CUB domain {132-248} MOTIF: N-glycosylation site {N213} N-glycosylation site {N237} N-glycosylation site {N242} cysteine residue {C250} MODIFICATION: cysteine residue {C260} N-glycosylation site {N253} cysteine residue {C254} MODIFICATION: cysteine residue {C271} cysteine residue {C260} MODIFICATION: cysteine residue {C250} N-glycosylation site {N264} cysteine residue {C271} MODIFICATION: cysteine residue {C254} cysteine residue {C273} MODIFICATION: cysteine residue {C282} cysteine residue {C282} MODIFICATION: cysteine residue {C273} N-glycosylation site {N300} N-glycosylation site {N325} kelch repeat {352-402} MOTIF: N-glycosylation site {N362} N-glycosylation site {N383} kelch repeat {404-451} MOTIF: N-glycosylation site {N416} N-glycosylation site {N428} kelch repeat {461-508} kelch repeat {513-564} kelch repeat {566-624} MOTIF: N-glycosylation site {N575} N-glycosylation site {N623} kelch repeat {625-671} N-glycosylation site {N731} C-TYPE LECTIN {795-919} MOTIF: cysteine residue {C816} MODIFICATION: cysteine residue {C918} N-glycosylation site {N863} N-glycosylation site {N914} cysteine residue {C918} MODIFICATION: cysteine residue {C816} N-glycosylation site {N923} N-glycosylation site {N986} N-glycosylation site {N1043} N-glycosylation site {N1054} EGF domain {1063-1108} MOTIF: cysteine residue {C1063} MODIFICATION: cysteine residue {C1071} cysteine residue {C1065} MODIFICATION: cysteine residue {C1077} cysteine residue {C1071} MODIFICATION: cysteine residue {C1063} N-glycosylation site {N1073} cysteine residue {C1077} MODIFICATION: cysteine residue {C1065} cysteine residue {C1080} MODIFICATION: cysteine residue {C1089} N-glycosylation site {N1082} cysteine residue {C1089} MODIFICATION: cysteine residue {C1080} cysteine residue {C1092} MODIFICATION: cysteine residue {C1106} cysteine residue {C1106} MODIFICATION: cysteine residue {C1092} EGF domain {1109-1157} MOTIF: cysteine residue {C1127} MODIFICATION: cysteine residue {C1137} cysteine residue {C1137} MODIFICATION: cysteine residue {C1127} cysteine residue {C1140} MODIFICATION: cysteine residue {C1155} cysteine residue {C1155} MODIFICATION: cysteine residue {C1140} N-glycosylation site {N1198} N-glycosylation site {N1206} N-glycosylation site {N1250} N-glycosylation site {N1259} transmembrane domain {1280-1300}

Database Correlations

OMIM 603130 UniProt O75882 PFAM correlations

References

UniProt :accession O75882