Full text data of AMIGO3
AMIGO3
(ALI3, KIAA1851)
[Confidence: low (only semi-automatic identification from reviews)]
Amphoterin-induced protein 3 (AMIGO-3; Alivin-3; Flags: Precursor)
Amphoterin-induced protein 3 (AMIGO-3; Alivin-3; Flags: Precursor)
UniProt
Q86WK7
ID AMGO3_HUMAN Reviewed; 504 AA.
AC Q86WK7; Q494V6; Q96JH6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2003, sequence version 1.
DT 22-JAN-2014, entry version 98.
DE RecName: Full=Amphoterin-induced protein 3;
DE AltName: Full=AMIGO-3;
DE AltName: Full=Alivin-3;
DE Flags: Precursor;
GN Name=AMIGO3; Synonyms=ALI3, KIAA1851; ORFNames=UNQ6084/PRO20089;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryonic kidney;
RX PubMed=12629050; DOI=10.1083/jcb.200209074;
RA Kuja-Panula J., Kiiltomaeki M., Yamashiro T., Rouhiainen A.,
RA 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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [3]
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.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics 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
RT project: 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
CC (By similarity).
CC -!- SUBUNIT: Binds AMIGO1 or AMIGO2 (By similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC protein (Potential).
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. AMIGO
CC family.
CC -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC domain.
CC -!- SIMILARITY: Contains 6 LRR (leucine-rich) repeats.
CC -!- SIMILARITY: Contains 1 LRRCT domain.
CC -!- SIMILARITY: Contains 1 LRRNT domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB47480.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_942015.1; NM_198722.2.
DR UniGene; Hs.567903; -.
DR ProteinModelPortal; Q86WK7; -.
DR SMR; Q86WK7; 32-369.
DR STRING; 9606.ENSP00000323096; -.
DR PhosphoSite; Q86WK7; -.
DR DMDM; 68052343; -.
DR PaxDb; Q86WK7; -.
DR PRIDE; Q86WK7; -.
DR Ensembl; ENST00000320431; ENSP00000323096; ENSG00000176020.
DR Ensembl; ENST00000535833; ENSP00000439268; ENSG00000176020.
DR GeneID; 386724; -.
DR KEGG; hsa:386724; -.
DR UCSC; uc003cxj.3; human.
DR CTD; 386724; -.
DR GeneCards; GC03M049729; -.
DR HGNC; HGNC:24075; AMIGO3.
DR HPA; HPA026673; -.
DR neXtProt; NX_Q86WK7; -.
DR PharmGKB; PA142672627; -.
DR eggNOG; NOG146733; -.
DR HOGENOM; HOG000231327; -.
DR HOVERGEN; HBG080231; -.
DR InParanoid; Q86WK7; -.
DR OMA; VCLATGP; -.
DR OrthoDB; EOG7C8GHP; -.
DR GenomeRNAi; 386724; -.
DR NextBio; 101050; -.
DR PRO; PR:Q86WK7; -.
DR CleanEx; HS_AMIGO3; -.
DR Genevestigator; Q86WK7; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR000372; LRR-contain_N.
DR SMART; SM00409; IG; 1.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 5.
PE 2: Evidence at transcript level;
KW Cell adhesion; Complete proteome; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Leucine-rich repeat; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 19 Potential.
FT CHAIN 20 504 Amphoterin-induced protein 3.
FT /FTId=PRO_0000014513.
FT TOPO_DOM 20 383 Extracellular (Potential).
FT TRANSMEM 384 404 Helical; (Potential).
FT TOPO_DOM 405 504 Cytoplasmic (Potential).
FT DOMAIN 25 61 LRRNT.
FT REPEAT 62 83 LRR 1.
FT REPEAT 86 107 LRR 2.
FT REPEAT 110 133 LRR 3.
FT REPEAT 134 155 LRR 4.
FT REPEAT 158 178 LRR 5.
FT REPEAT 184 207 LRR 6.
FT DOMAIN 219 275 LRRCT.
FT DOMAIN 277 370 Ig-like C2-type.
FT CARBOHYD 107 107 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 272 272 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 301 301 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 362 362 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 368 368 N-linked (GlcNAc...) (Potential).
FT DISULFID 34 40 By similarity.
FT DISULFID 38 47 By similarity.
FT DISULFID 223 251 By similarity.
FT DISULFID 225 273 By similarity.
FT DISULFID 300 352 By similarity.
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
//
ID AMGO3_HUMAN Reviewed; 504 AA.
AC Q86WK7; Q494V6; Q96JH6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2003, sequence version 1.
DT 22-JAN-2014, entry version 98.
DE RecName: Full=Amphoterin-induced protein 3;
DE AltName: Full=AMIGO-3;
DE AltName: Full=Alivin-3;
DE Flags: Precursor;
GN Name=AMIGO3; Synonyms=ALI3, KIAA1851; ORFNames=UNQ6084/PRO20089;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryonic kidney;
RX PubMed=12629050; DOI=10.1083/jcb.200209074;
RA Kuja-Panula J., Kiiltomaeki M., Yamashiro T., Rouhiainen A.,
RA 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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [3]
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.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics 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
RT project: 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
CC (By similarity).
CC -!- SUBUNIT: Binds AMIGO1 or AMIGO2 (By similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC protein (Potential).
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. AMIGO
CC family.
CC -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC domain.
CC -!- SIMILARITY: Contains 6 LRR (leucine-rich) repeats.
CC -!- SIMILARITY: Contains 1 LRRCT domain.
CC -!- SIMILARITY: Contains 1 LRRNT domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB47480.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_942015.1; NM_198722.2.
DR UniGene; Hs.567903; -.
DR ProteinModelPortal; Q86WK7; -.
DR SMR; Q86WK7; 32-369.
DR STRING; 9606.ENSP00000323096; -.
DR PhosphoSite; Q86WK7; -.
DR DMDM; 68052343; -.
DR PaxDb; Q86WK7; -.
DR PRIDE; Q86WK7; -.
DR Ensembl; ENST00000320431; ENSP00000323096; ENSG00000176020.
DR Ensembl; ENST00000535833; ENSP00000439268; ENSG00000176020.
DR GeneID; 386724; -.
DR KEGG; hsa:386724; -.
DR UCSC; uc003cxj.3; human.
DR CTD; 386724; -.
DR GeneCards; GC03M049729; -.
DR HGNC; HGNC:24075; AMIGO3.
DR HPA; HPA026673; -.
DR neXtProt; NX_Q86WK7; -.
DR PharmGKB; PA142672627; -.
DR eggNOG; NOG146733; -.
DR HOGENOM; HOG000231327; -.
DR HOVERGEN; HBG080231; -.
DR InParanoid; Q86WK7; -.
DR OMA; VCLATGP; -.
DR OrthoDB; EOG7C8GHP; -.
DR GenomeRNAi; 386724; -.
DR NextBio; 101050; -.
DR PRO; PR:Q86WK7; -.
DR CleanEx; HS_AMIGO3; -.
DR Genevestigator; Q86WK7; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR000372; LRR-contain_N.
DR SMART; SM00409; IG; 1.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 5.
PE 2: Evidence at transcript level;
KW Cell adhesion; Complete proteome; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Leucine-rich repeat; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 19 Potential.
FT CHAIN 20 504 Amphoterin-induced protein 3.
FT /FTId=PRO_0000014513.
FT TOPO_DOM 20 383 Extracellular (Potential).
FT TRANSMEM 384 404 Helical; (Potential).
FT TOPO_DOM 405 504 Cytoplasmic (Potential).
FT DOMAIN 25 61 LRRNT.
FT REPEAT 62 83 LRR 1.
FT REPEAT 86 107 LRR 2.
FT REPEAT 110 133 LRR 3.
FT REPEAT 134 155 LRR 4.
FT REPEAT 158 178 LRR 5.
FT REPEAT 184 207 LRR 6.
FT DOMAIN 219 275 LRRCT.
FT DOMAIN 277 370 Ig-like C2-type.
FT CARBOHYD 107 107 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 272 272 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 301 301 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 362 362 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 368 368 N-linked (GlcNAc...) (Potential).
FT DISULFID 34 40 By similarity.
FT DISULFID 38 47 By similarity.
FT DISULFID 223 251 By similarity.
FT DISULFID 225 273 By similarity.
FT DISULFID 300 352 By similarity.
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
//