ID AMGO2_PONAB Reviewed; 522 AA.
AC Q5R7M3;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-MAY-2023, entry version 89.
DE RecName: Full=Amphoterin-induced protein 2;
DE AltName: Full=AMIGO-2;
DE Flags: Precursor;
GN Name=AMIGO2 {ECO:0000250|UniProtKB:Q7TNJ4};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1] {ECO:0000312|EMBL:CAH92237.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:CAH92237.1};
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for depolarization-dependent survival of cultured
CC cerebellar granule neurons. May mediate homophilic as well as
CC heterophilic cell-cell interaction with AMIGO1 or AMIGO3. May
CC contribute to signal transduction through its intracellular domain (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds itself as well as AMIGO1 and AMIGO3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Note=Associated
CC with nucleus as well as plasma membrane. Restricted to somata of
CC cerebellar as well as hippocampal neurons (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. AMIGO family.
CC {ECO:0000305}.
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DR EMBL; CR860091; CAH92237.1; -; mRNA.
DR AlphaFoldDB; Q5R7M3; -.
DR SMR; Q5R7M3; -.
DR STRING; 9601.ENSPPYP00000005068; -.
DR GlyCosmos; Q5R7M3; 7 sites, No reported glycans.
DR eggNOG; ENOG502R009; Eukaryota.
DR InParanoid; Q5R7M3; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0043069; P:negative regulation of programmed cell death; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR031283; AMIGO.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR24368; AMPHOTERIN-INDUCED PROTEIN; 1.
DR PANTHER; PTHR24368:SF209; AMPHOTERIN-INDUCED PROTEIN 2; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00082; LRRCT; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 6.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Leucine-rich repeat; Membrane; Nucleus;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..522
FT /note="Amphoterin-induced protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014511"
FT TOPO_DOM 40..398
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 40..68
FT /note="LRRNT"
FT REPEAT 69..90
FT /note="LRR 1"
FT REPEAT 94..115
FT /note="LRR 2"
FT REPEAT 118..139
FT /note="LRR 3"
FT REPEAT 142..163
FT /note="LRR 4"
FT REPEAT 166..187
FT /note="LRR 5"
FT REPEAT 193..214
FT /note="LRR 6"
FT DOMAIN 228..284
FT /note="LRRCT"
FT DOMAIN 289..379
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255"
FT REGION 501..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 45..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 232..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 234..282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 310..363
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 522 AA; 57897 MW; F34306196424E300 CRC64;
MSLRVHTLPT LLGAVVRPGC RELLCLLMIT VAVGPGASGV CPTACICATD IVSCTNKHLS
KVPGNLFRLM KRLDLSYNRI GLLDSEWIPV SFAKLNTLIL RHNNITSIST GSFSTTPNLK
CLDLSSNKLK TVKNAVFQEL KVLEVLLLYN NHISYLDPSA FGGLSQLQKL YLSGNFLTQF
PMDLYVGRFK LAELMFLDVS YNRIPSMPMH HINLVPGKQL RGIYLHGNPF VCDCSLYSLL
VFWYRRHFSS VMDFKNDYTC RLWSDSRHSR QVLLLQDSFM NCSDSIINGS FRALGFIHEA
QVGERLMVHC DSKTGNANTD FIWVGPDNRL LEPDKEMENF YVFHNGSLVI ESPRFEDAGV
YSCIAMNKQR LLNETVDVTI NVSNVTVSRS HAHEAFNTAF TTLAACVASI VLVLLYLYLT
PCPCKCKTKR QKNMLHQSNA HSSILSPGPA SDASADERKA GAGKRVVFLE PLKDTAAGQN
GKVRLFPSEA VIAEGILKST RGKSDSDSVN SVFSDTPFVA ST
//
