amphoterin-induced protein 2 (AMIGO-2, alivin-1, differentially expressed in gastric adenocarcinomas, DEGA, AMIGO2, ALI1)

Function: - required for depolarization-dependent survival of cultured cerebellar granule neurons - may mediate homophilic & heterophilic cell-cell interaction with AMIGO1 or AMIGO3 - may contribute to signal transduction through its intracellular domain - binds itself as well as AMIGO1 & AMIGO3 Structure: - belongs to the immunoglobulin superfamily, AMIGO family - contains 1 Ig-like C2-type (immunoglobulin-like) domain - contains 6 LRR (leucine-rich) repeats Compartment: - cell membrane, nucleus - restricted to somata of cerebellar & hippocampal neurons Expression: - expressed in breast, ovary, cervix, uterus > lung, colon, rectum Pathology: - differentially expressed in 56% of thyroid cancers 57% of pancreatic cancer 45% of stomach cancer

Properties

SIZE: MW = 58 kD entity length = 522 aa COMPARTMENT: cell nucleus MOTIF: signal sequence {1-39} N-glycosylation site {N58} leucine-rich repeat SITE: 67-90 MOTIF: leucine residue (SEVERAL) leucine-rich repeat SITE: 92-115 MOTIF: leucine residue (SEVERAL) N-glycosylation site {N104} leucine-rich repeat SITE: 116-139 MOTIF: leucine residue (SEVERAL) leucine-rich repeat SITE: 141-163 MOTIF: leucine residue (SEVERAL) leucine-rich repeat SITE: 164-187 MOTIF: leucine residue (SEVERAL) leucine-rich repeat SITE: 191-214 MOTIF: leucine residue (SEVERAL) N-glycosylation site {N281} N-glycosylation site {N288} immunoglobulin superfamily domain {289-379} MOTIF: cysteine residue {C310} MODIFICATION: cysteine residue {C363} N-glycosylation site {N345} cysteine residue {C363} MODIFICATION: cysteine residue {C310} N-glycosylation site {N373} N-glycosylation site {N381} N-glycosylation site {N384} transmembrane domain {399-419}

Database Correlations

UniProt Q86SJ2 PFAM correlations

References

UniProt :accession Q86SJ2