AMGO3_MOUSE
ID AMGO3_MOUSE Reviewed; 508 AA.
AC Q8C2S7; Q6ZPH1; Q8CEB3;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
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|MGI:MGI:2444854};
GN Synonyms=Ali3 {ECO:0000312|EMBL:BAD12542.1},
GN Kiaa1851 {ECO:0000312|EMBL:BAC98266.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAO48945.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAO48945.1};
RC TISSUE=Cerebellum {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:BAD12542.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:BAD12542.1};
RA Ono T.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Skin, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4] {ECO:0000312|EMBL:BAC98266.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail {ECO:0000312|EMBL:BAC98266.1};
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
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 -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12629050}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. AMIGO family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC26035.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC98266.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY237004; AAO48945.1; -; mRNA.
DR EMBL; AB167510; BAD12542.1; -; mRNA.
DR EMBL; AK028619; BAC26035.1; ALT_FRAME; mRNA.
DR EMBL; AK088051; BAC40120.1; -; mRNA.
DR EMBL; AK129456; BAC98266.1; ALT_INIT; mRNA.
DR CCDS; CCDS23516.1; -.
DR RefSeq; NP_796249.1; NM_177275.4.
DR AlphaFoldDB; Q8C2S7; -.
DR SMR; Q8C2S7; -.
DR BioGRID; 236335; 1.
DR STRING; 10090.ENSMUSP00000082137; -.
DR GlyGen; Q8C2S7; 6 sites.
DR iPTMnet; Q8C2S7; -.
DR PhosphoSitePlus; Q8C2S7; -.
DR PaxDb; Q8C2S7; -.
DR PRIDE; Q8C2S7; -.
DR ProteomicsDB; 296028; -.
DR Antibodypedia; 13729; 140 antibodies from 23 providers.
DR DNASU; 320844; -.
DR Ensembl; ENSMUST00000085060; ENSMUSP00000082137; ENSMUSG00000032593.
DR GeneID; 320844; -.
DR KEGG; mmu:320844; -.
DR UCSC; uc009rom.1; mouse.
DR CTD; 386724; -.
DR MGI; MGI:2444854; Amigo3.
DR VEuPathDB; HostDB:ENSMUSG00000032593; -.
DR eggNOG; ENOG502QUWU; Eukaryota.
DR GeneTree; ENSGT00950000183146; -.
DR HOGENOM; CLU_030478_0_0_1; -.
DR InParanoid; Q8C2S7; -.
DR OMA; PQECSAQ; -.
DR OrthoDB; 54386at2759; -.
DR PhylomeDB; Q8C2S7; -.
DR TreeFam; TF326838; -.
DR BioGRID-ORCS; 320844; 6 hits in 72 CRISPR screens.
DR PRO; PR:Q8C2S7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8C2S7; protein.
DR Bgee; ENSMUSG00000032593; Expressed in humerus cartilage element and 61 other tissues.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; ISO:MGI.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
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; 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; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 7.
PE 1: Evidence at protein 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..508
FT /note="Amphoterin-induced protein 3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014514"
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..508
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 279..370
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
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 508 AA; 55625 MW; 31334E42F91810C5 CRC64;
MAWLVLSGIL LCMLGAGLGT SDLEDVLPPA PHNCPDICIC AADVLSCAGR GLQDLPVALP
TTAAELDLSH NALKRLHPGW LAPLSRLRAL HLGYNKLEVL GHGAFTNASG LRTLDLSSNM
LRMLHTHDLD GLEELEKLLL FNNSLMHLDL DAFQGLRMLS HLYLSCNELS SFSFNHLHGL
GLTRLRTLDL SSNWLKHISI PELAALPTYL KNRLYLHNNP LPCDCSLYHL LRRWHQRGLS
ALHDFEREYT CLVFKVSESR VRFFEHSRVF KNCSVAAAPG LELPEEQLHA QVGQSLRLFC
NTSVPATRVA WVSPKNELLV APASQDGSIA VLADGSLAIG RVQEQHAGVF VCLASGPRLH
HNQTLEYNVS VQKARPEPET FNTGFTTLLG CIVGLVLVLL YLFAPPCRGC CHCCQRACRN
RCWPRASSPL QELSAQSSML STTPPDAPSR KASVHKHVVF LEPGKKGLNG RVQLAVAEDF
DLCNPMGLQL KAGSESASST GSEGLVMS
