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AMGO3_HUMAN
ID   AMGO3_HUMAN             Reviewed;         504 AA.
AC   Q86WK7; Q494V6; Q96JH6;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Amphoterin-induced protein 3;
DE   AltName: Full=AMIGO-3;
DE   AltName: Full=Alivin-3;
DE   Flags: Precursor;
GN   Name=AMIGO3 {ECO:0000312|EMBL:AAO48944.1};
GN   Synonyms=ALI3 {ECO:0000250|UniProtKB:Q8C2S7},
GN   KIAA1851 {ECO:0000312|EMBL:BAB47480.1}; ORFNames=UNQ6084/PRO20089;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1] {ECO:0000312|EMBL:AAO48944.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryonic kidney {ECO:0000269|PubMed:12629050};
RX   PubMed=12629050; DOI=10.1083/jcb.200209074;
RA   Kuja-Panula J., Kiiltomaeki M., Yamashiro T., Rouhiainen A., Rauvala H.;
RT   "AMIGO, a transmembrane protein implicated in axon tract development,
RT   defines a novel protein family with leucine-rich repeats.";
RL   J. Cell Biol. 160:963-973(2003).
RN   [2] {ECO:0000312|EMBL:BAB47480.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000312|EMBL:BAB47480.1};
RX   PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA   Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XX. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 8:85-95(2001).
RN   [3] {ECO:0000312|EMBL:AAQ88501.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May mediate heterophilic cell-cell interaction. May
CC       contribute to signal transduction through its intracellular domain (By
CC       similarity). {ECO:0000250|UniProtKB:Q80ZD5}.
CC   -!- SUBUNIT: Binds AMIGO1 or AMIGO2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. AMIGO family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB47480.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY237003; AAO48944.1; -; mRNA.
DR   EMBL; AB058754; BAB47480.1; ALT_INIT; mRNA.
DR   EMBL; AY358134; AAQ88501.1; -; mRNA.
DR   EMBL; BC101363; AAI01364.1; -; mRNA.
DR   EMBL; BC101364; AAI01365.1; -; mRNA.
DR   CCDS; CCDS33759.1; -.
DR   RefSeq; NP_942015.1; NM_198722.2.
DR   AlphaFoldDB; Q86WK7; -.
DR   SMR; Q86WK7; -.
DR   BioGRID; 132150; 37.
DR   IntAct; Q86WK7; 12.
DR   STRING; 9606.ENSP00000323096; -.
DR   GlyGen; Q86WK7; 5 sites.
DR   iPTMnet; Q86WK7; -.
DR   PhosphoSitePlus; Q86WK7; -.
DR   BioMuta; AMIGO3; -.
DR   DMDM; 68052343; -.
DR   MassIVE; Q86WK7; -.
DR   PaxDb; Q86WK7; -.
DR   PeptideAtlas; Q86WK7; -.
DR   PRIDE; Q86WK7; -.
DR   ProteomicsDB; 70179; -.
DR   Antibodypedia; 13729; 140 antibodies from 23 providers.
DR   DNASU; 386724; -.
DR   Ensembl; ENST00000320431.8; ENSP00000323096.7; ENSG00000176020.9.
DR   GeneID; 386724; -.
DR   KEGG; hsa:386724; -.
DR   MANE-Select; ENST00000320431.8; ENSP00000323096.7; NM_198722.3; NP_942015.1.
DR   UCSC; uc003cxj.4; human.
DR   CTD; 386724; -.
DR   DisGeNET; 386724; -.
DR   GeneCards; AMIGO3; -.
DR   HGNC; HGNC:24075; AMIGO3.
DR   HPA; ENSG00000176020; Low tissue specificity.
DR   MIM; 615691; gene.
DR   neXtProt; NX_Q86WK7; -.
DR   PharmGKB; PA142672627; -.
DR   VEuPathDB; HostDB:ENSG00000176020; -.
DR   eggNOG; ENOG502QUWU; Eukaryota.
DR   GeneTree; ENSGT00950000183146; -.
DR   HOGENOM; CLU_030478_0_0_1; -.
DR   InParanoid; Q86WK7; -.
DR   OMA; PQECSAQ; -.
DR   OrthoDB; 564038at2759; -.
DR   PhylomeDB; Q86WK7; -.
DR   TreeFam; TF326838; -.
DR   PathwayCommons; Q86WK7; -.
DR   SignaLink; Q86WK7; -.
DR   BioGRID-ORCS; 386724; 13 hits in 1022 CRISPR screens.
DR   GenomeRNAi; 386724; -.
DR   Pharos; Q86WK7; Tdark.
DR   PRO; PR:Q86WK7; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q86WK7; protein.
DR   Bgee; ENSG00000176020; Expressed in hindlimb stylopod muscle and 89 other tissues.
DR   Genevisible; Q86WK7; HS.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0007420; P:brain development; IBA:GO_Central.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR031283; AMIGO.
DR   InterPro; IPR031285; AMIGO3.
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; IPR003598; Ig_sub2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR24368; PTHR24368; 1.
DR   PANTHER; PTHR24368:SF62; PTHR24368:SF62; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00369; LRR_TYP; 6.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51450; LRR; 5.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Leucine-rich repeat; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..504
FT                   /note="Amphoterin-induced protein 3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000014513"
FT   TOPO_DOM        20..383
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        405..504
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          25..61
FT                   /note="LRRNT"
FT   REPEAT          62..83
FT                   /note="LRR 1"
FT   REPEAT          86..107
FT                   /note="LRR 2"
FT   REPEAT          110..133
FT                   /note="LRR 3"
FT   REPEAT          134..155
FT                   /note="LRR 4"
FT   REPEAT          158..178
FT                   /note="LRR 5"
FT   REPEAT          184..207
FT                   /note="LRR 6"
FT   DOMAIN          219..275
FT                   /note="LRRCT"
FT   DOMAIN          277..370
FT                   /note="Ig-like C2-type"
FT                   /evidence="ECO:0000255"
FT   REGION          422..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        368
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        34..40
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        38..47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        223..251
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        225..273
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        300..352
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   504 AA;  55250 MW;  92044CA180BD34FA CRC64;
     MTWLVLLGTL LCMLRVGLGT PDSEGFPPRA LHNCPYKCIC AADLLSCTGL GLQDVPAELP
     AATADLDLSH NALQRLRPGW LAPLFQLRAL HLDHNELDAL GRGVFVNASG LRLLDLSSNT
     LRALGRHDLD GLGALEKLLL FNNRLVHLDE HAFHGLRALS HLYLGCNELA SFSFDHLHGL
     SATHLLTLDL SSNRLGHISV PELAALPAFL KNGLYLHNNP LPCDCRLYHL LQRWHQRGLS
     AVRDFAREYV CLAFKVPASR VRFFQHSRVF ENCSSAPALG LERPEEHLYA LVGRSLRLYC
     NTSVPAMRIA WVSPQQELLR APGSRDGSIA VLADGSLAIG NVQEQHAGLF VCLATGPRLH
     HNQTHEYNVS VHFPRPEPEA FNTGFTTLLG CAVGLVLVLL YLFAPPCRCC RRACRCRRWP
     QTPSPLQELS AQSSVLSTTP PDAPSRKASV HKHVVFLEPG RRGLNGRVQL AVAEEFDLYN
     PGGLQLKAGS ESASSIGSEG PMTT
 
 
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