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attractin-like protein 1 (ATRNL1, KIAA0534)
Function:
- may play a role in melanocortin signaling pathways that regulate energy homeostasis
- interacts with MC4R (putative)
Structure:
- contains 1 C-type lectin domain
- contains 1 CUB domain
- contains 2 EGF-like domains
- contains 6 kelch repeats
- contains 2 laminin EGF-like domains
- contains 5 PSI domains
Compartment: membrane (putative)
Alternative splicing: named isoforms=2
General
glycoprotein
lectin
membrane protein
Properties
SIZE: entity length = 1379 aa
MW = 153 kD
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-52}
EGF domain {53-91}
MOTIF: cysteine residue {C63}
MODIFICATION: cysteine residue {C79}
N-glycosylation site {N76}
cysteine residue {C79}
MODIFICATION: cysteine residue {C63}
cysteine residue {C81}
MODIFICATION: cysteine residue {C90}
cysteine residue {C90}
MODIFICATION: cysteine residue {C81}
CUB domain {93-209}
MOTIF: cysteine residue {C93}
MODIFICATION: cysteine residue {C119}
cysteine residue {C119}
MODIFICATION: cysteine residue {C93}
N-glycosylation site {N174}
N-glycosylation site {N198}
EGF domain {207-245}
MOTIF: cysteine residue {C211}
MODIFICATION: cysteine residue {C221}
cysteine residue {C215}
MODIFICATION: cysteine residue {C233}
cysteine residue {C221}
MODIFICATION: cysteine residue {C211}
cysteine residue {C233}
MODIFICATION: cysteine residue {C215}
cysteine residue {C235}
MODIFICATION: cysteine residue {C244}
cysteine residue {C244}
MODIFICATION: cysteine residue {C235}
kelch repeat {316-365}
kelch repeat {367-415}
MOTIF: N-glycosylation site {N380}
kelch repeat {427-475}
kelch repeat {480-531}
kelch repeat {533-591}
kelch repeat {592-638}
PSI 1 {614-657}
PSI 2 {666-709}
PSI 3 {715-760}
C-type lectin {755-873}
MOTIF: N-glycosylation site {N763}
cysteine residue {C776}
MODIFICATION: cysteine residue {C872}
N-glycosylation site {N778}
cysteine residue {C872}
MODIFICATION: cysteine residue {C776}
PSI 4 {889-939}
MOTIF: N-glycosylation site {N898}
PSI 5 {942-1012}
EGF domain {1014-1059}
MOTIF: cysteine residue {C1014}
MODIFICATION: cysteine residue {C1022}
cysteine residue {C1016}
MODIFICATION: cysteine residue {C1028}
cysteine residue {C1022}
MODIFICATION: cysteine residue {C1014}
cysteine residue {C1028}
MODIFICATION: cysteine residue {C1016}
cysteine residue {C1031}
MODIFICATION: cysteine residue {C1040}
cysteine residue {C1040}
MODIFICATION: cysteine residue {C1031}
cysteine residue {C1043}
MODIFICATION: cysteine residue {C1057}
cysteine residue {C1057}
MODIFICATION: cysteine residue {C1043}
EGF domain {1060-1108}
MOTIF: cysteine residue {C1060}
MODIFICATION: cysteine residue {C1069}
cysteine residue {C1062}
MODIFICATION: cysteine residue {C1076}
cysteine residue {C1069}
MODIFICATION: cysteine residue {C1060}
cysteine residue {C1076}
MODIFICATION: cysteine residue {C1062}
cysteine residue {C1078}
MODIFICATION: cysteine residue {C1088}
cysteine residue {C1088}
MODIFICATION: cysteine residue {C1078}
cysteine residue {C1091}
MODIFICATION: cysteine residue {C1106}
cysteine residue {C1106}
MODIFICATION: cysteine residue {C1091}
N-glycosylation site {N1157}
transmembrane domain {1231-1251}
Database Correlations
UniProt Q5VV63
PFAM correlations
Kegg hsa:2603
References
UniProt :accession Q5VV63