ASTN1_MOUSE
ID ASTN1_MOUSE Reviewed; 1302 AA.
AC Q61137; G5E8A1; Q505A0; Q7TQG3; Q8CHH2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 4.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Astrotactin-1;
DE AltName: Full=Neuronal migration protein GC14;
DE Flags: Precursor;
GN Name=Astn1; Synonyms=Astn, Kiaa0289;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 44-1302 (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=8602532; DOI=10.1126/science.272.5260.417;
RA Zheng C., Heintz N., Hatten M.E.;
RT "CNS gene encoding astrotactin, which supports neuronal migration along
RT glial fibers.";
RL Science 272:417-419(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 46-1302 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [6]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11861479; DOI=10.1242/dev.129.4.965;
RA Adams N.C., Tomoda T., Cooper M., Dietz G., Hatten M.E.;
RT "Mice that lack astrotactin have slowed neuronal migration.";
RL Development 129:965-972(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP SUBCELLULAR LOCATION, INTERACTION WITH ASTN2, DEVELOPMENTAL STAGE, AND
RP TOPOLOGY.
RX PubMed=20573900; DOI=10.1523/jneurosci.0032-10.2010;
RA Wilson P.M., Fryer R.H., Fang Y., Hatten M.E.;
RT "Astn2, a novel member of the astrotactin gene family, regulates the
RT trafficking of ASTN1 during glial-guided neuronal migration.";
RL J. Neurosci. 30:8529-8540(2010).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-337, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Neuronal adhesion molecule that is required for normal
CC migration of young postmitotic neuroblasts along glial fibers,
CC especially in the cerebellum. Required for normal rate of migration of
CC granule cells during brain development and for normal cerebellum
CC development. {ECO:0000269|PubMed:11861479, ECO:0000269|PubMed:8602532}.
CC -!- SUBUNIT: Interacts with ASTN2; the interaction is not calcium-
CC dependent. {ECO:0000269|PubMed:20573900}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20573900,
CC ECO:0000269|PubMed:8602532}; Multi-pass membrane protein {ECO:0000305}.
CC Perikaryon {ECO:0000269|PubMed:20573900}. Endosome
CC {ECO:0000269|PubMed:20573900}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000305|PubMed:20573900}. Note=Detected close to the
CC anterior pole and at the base of the leading process in migrating
CC neurons. Is internalized from the membrane via clathrin-coated vesicles
CC and endosomes, and recycled to the anterior pole of the migrating cell.
CC {ECO:0000269|PubMed:20573900}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q61137-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61137-2; Sequence=VSP_014917;
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level)
CC (PubMed:11861479). Expressed specifically in the brain. Expressed in
CC the cerebellum, hippocampus, cerebrum and olfactory bulb
CC (PubMed:8602532). {ECO:0000269|PubMed:11861479,
CC ECO:0000269|PubMed:8602532}.
CC -!- DEVELOPMENTAL STAGE: First detected in embryonic brain at 12 dpc.
CC Expression increases thereafter, is highest in brain from pups 4 days
CC after birth, and then decreases again. Expression is decreased 14 days
CC after birth, and not detectable in adult brain.
CC {ECO:0000269|PubMed:20573900}.
CC -!- DISRUPTION PHENOTYPE: Slower than normal migration of granule cells in
CC the developing cerebellum, leading to a decreased cerebellum size in
CC adult mice and impaired skills in tasks that require coordinated
CC movement and balance. Granule cells from mutant mice have a rounded
CC shape and lack the elongated shape seen in wild-type. At 6 days after
CC birth, increased granule cell apoptosis is observed, contrary to the
CC situation in wild-type. {ECO:0000269|PubMed:11861479}.
CC -!- SIMILARITY: Belongs to the astrotactin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52516.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC091266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC118728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC119867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC158910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466520; EDL39354.1; -; Genomic_DNA.
DR EMBL; BC054545; AAH54545.1; -; mRNA.
DR EMBL; BC094666; AAH94666.1; -; mRNA.
DR EMBL; U48797; AAC52516.1; ALT_FRAME; mRNA.
DR EMBL; AB093222; BAC41406.2; -; mRNA.
DR CCDS; CCDS56648.1; -. [Q61137-1]
DR CCDS; CCDS78721.1; -. [Q61137-2]
DR RefSeq; NP_001192133.1; NM_001205204.1. [Q61137-1]
DR RefSeq; NP_031521.2; NM_007495.4. [Q61137-2]
DR AlphaFoldDB; Q61137; -.
DR SMR; Q61137; -.
DR BioGRID; 198227; 1.
DR IntAct; Q61137; 2.
DR MINT; Q61137; -.
DR STRING; 10090.ENSMUSP00000039711; -.
DR GlyGen; Q61137; 6 sites.
DR iPTMnet; Q61137; -.
DR PhosphoSitePlus; Q61137; -.
DR MaxQB; Q61137; -.
DR PaxDb; Q61137; -.
DR PRIDE; Q61137; -.
DR ProteomicsDB; 281861; -. [Q61137-1]
DR ProteomicsDB; 281862; -. [Q61137-2]
DR Antibodypedia; 55629; 20 antibodies from 12 providers.
DR DNASU; 11899; -.
DR Ensembl; ENSMUST00000046110; ENSMUSP00000039711; ENSMUSG00000026587. [Q61137-2]
DR Ensembl; ENSMUST00000193042; ENSMUSP00000142322; ENSMUSG00000026587. [Q61137-1]
DR GeneID; 11899; -.
DR KEGG; mmu:11899; -.
DR UCSC; uc007ddu.3; mouse. [Q61137-1]
DR CTD; 460; -.
DR MGI; MGI:1098567; Astn1.
DR VEuPathDB; HostDB:ENSMUSG00000026587; -.
DR eggNOG; ENOG502R4QT; Eukaryota.
DR GeneTree; ENSGT00390000003140; -.
DR HOGENOM; CLU_006316_1_0_1; -.
DR InParanoid; Q61137; -.
DR OMA; ISMIVRC; -.
DR OrthoDB; 39300at2759; -.
DR PhylomeDB; Q61137; -.
DR TreeFam; TF332034; -.
DR BioGRID-ORCS; 11899; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q61137; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q61137; protein.
DR Bgee; ENSMUSG00000026587; Expressed in subiculum and 166 other tissues.
DR ExpressionAtlas; Q61137; baseline and differential.
DR Genevisible; Q61137; MM.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0016477; P:cell migration; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0007158; P:neuron cell-cell adhesion; IDA:MGI.
DR GO; GO:0001764; P:neuron migration; IDA:MGI.
DR CDD; cd00063; FN3; 1.
DR InterPro; IPR040685; Annexin-like.
DR InterPro; IPR045574; ASTN1_2_EGF_Fn.
DR InterPro; IPR045575; ASTN_1_2_N.
DR InterPro; IPR026995; Astrotactin.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR020864; MACPF.
DR PANTHER; PTHR16592; PTHR16592; 1.
DR Pfam; PF18411; Annexin_like; 1.
DR Pfam; PF19743; ASTN1_2_EGF_Fn; 1.
DR Pfam; PF19441; ASTN_1_2_N; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00457; MACPF; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Cytoplasmic vesicle;
KW Disulfide bond; EGF-like domain; Endosome; Glycoprotein; Membrane;
KW Methylation; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1302
FT /note="Astrotactin-1"
FT /id="PRO_0000007482"
FT TOPO_DOM 22..153
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..1302
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:20573900, ECO:0000305"
FT DOMAIN 459..507
FT /note="EGF-like 1"
FT DOMAIN 608..652
FT /note="EGF-like 2"
FT DOMAIN 656..708
FT /note="EGF-like 3"
FT DOMAIN 1030..1145
FT /note="Fibronectin type-III"
FT REGION 340..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 337
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 729
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 742
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 804
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 984
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 463..475
FT /evidence="ECO:0000250"
FT DISULFID 471..490
FT /evidence="ECO:0000250"
FT DISULFID 492..506
FT /evidence="ECO:0000250"
FT DISULFID 612..625
FT /evidence="ECO:0000250"
FT DISULFID 619..636
FT /evidence="ECO:0000250"
FT DISULFID 638..651
FT /evidence="ECO:0000250"
FT DISULFID 660..672
FT /evidence="ECO:0000250"
FT DISULFID 668..692
FT /evidence="ECO:0000250"
FT DISULFID 694..707
FT /evidence="ECO:0000250"
FT DISULFID 785..951
FT /evidence="ECO:0000250|UniProtKB:O75129"
FT DISULFID 876..941
FT /evidence="ECO:0000250|UniProtKB:O75129"
FT DISULFID 947..954
FT /evidence="ECO:0000250|UniProtKB:O75129"
FT DISULFID 1000..1011
FT /evidence="ECO:0000250|UniProtKB:O75129"
FT DISULFID 1013..1026
FT /evidence="ECO:0000250|UniProtKB:O75129"
FT DISULFID 1101..1121
FT /evidence="ECO:0000250|UniProtKB:O75129"
FT DISULFID 1153..1240
FT /evidence="ECO:0000250|UniProtKB:O75129"
FT DISULFID 1261..1284
FT /evidence="ECO:0000250|UniProtKB:O75129"
FT VAR_SEQ 480..487
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12465718,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_014917"
FT CONFLICT 216
FT /note="S -> T (in Ref. 4; AAC52516)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="R -> L (in Ref. 4; AAC52516)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="I -> L (in Ref. 5; BAC41406)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="I -> M (in Ref. 3; AAH94666)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="A -> R (in Ref. 4; AAC52516)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="E -> D (in Ref. 5; BAC41406)"
FT /evidence="ECO:0000305"
FT CONFLICT 1045
FT /note="N -> T (in Ref. 5; BAC41406)"
FT /evidence="ECO:0000305"
FT CONFLICT 1067
FT /note="I -> Y (in Ref. 4; AAC52516)"
FT /evidence="ECO:0000305"
FT CONFLICT 1214
FT /note="Missing (in Ref. 4; AAC52516)"
FT /evidence="ECO:0000305"
FT CONFLICT 1260..1261
FT /note="GC -> AG (in Ref. 4; AAC52516)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1302 AA; 144884 MW; AC917C4281401C97 CRC64;
MALAGLCALF ACCWGPAAVL ATAAGDVDPS KELECKLKSI TVSALPFLRE NDLSIMHSPS
ASEPKLLFSV RNDFPGEMVV VDDLENTELP YFVLEISGNT EDIPLVRWRQ QWLENGTLLF
HIHHQDGAPS LPGQDPTEEP QHESAEEELR ILHISVMGGM IALLLSILCL VMILYTRRRW
CKRRRVPQPQ KSASAEAANE IHYIPSVLIG GHGRESLRNA RVQGHNSSGT LSIRETPILD
GYEYDITDLR HHLQRECMNG GEDFASQVTR TLDSLQGCNE KSGMDLTPGS DNAKLSLMNK
YKDNIIATSP VDSNHQQATL LSHTSSSQRK RINNKARAGS AFLNPEGDSS TEAENDPQLT
FYTDPSRSRR RSRVGSPRSP VNKTTLTLIS VTSCVIGLVC SSHVSCPLVV KITLHVPEHL
IADGSRFILL EGSQLDASDW LNPAQVVLFS QQNSSGPWAM DLCARRLLDP CEHQCDPETG
RREHRAAGEC LCYEGYMKDP VHKHLCIRNE WGTNQGPWPY TIFQRGFDLV LGEQPSDKIF
RFTYTLGEGM WLPLSKSFVI PPAELAINPS AKCKTDMTVM EDAVEVREEL MTSSSFDSLE
VLLDSFGPVR DCSKDNGGCS KNFRCISDRK LDSTGCVCPS GLSPMKDSSG CYDRHIGVDC
SDGFNGGCEQ LCLQQMAPFP EDPTLYNILM FCGCIEDYKL GVDGRSCQLV TETCPEGGDC
GESREVPMNQ TLFGEMFFGY NNQSKEVATG QVLKGTFRQN NFARGLDQQL PDGLVVASVP
LENQCLEEIS EPTPDPDFLT GMVNFSEVSG YPVLQHWKVR SVMYHIKLNQ AAISQAFSNA
LHSLDGATSR ADFVALLDQF GNHYIQEAVY GFEESCSIWY PNKQVQRRLW LEYEDISKGN
SPSDESEERE RDPKVLTFPE YIASLSDSGT KRMAAGVRME CQSKGRCPSS CPLCHVTSSP
ETPAEPVLLE VTRASPIYEL VTNNQTQRLL QEATMSSLWC SGTGDVIEDW CRCDSTAFGA
DGLPTCAPLP QPVLRLSTVH EPSSNLVVLE WEHSEPPIGV QIVDYLIRQE KVTDRMDHSK
VETETVLSFV DDIISGAKAP CAMPSQVPDK QLTTISLIIR CLEPDTIYMF TLWGVDNTGR
RSRPSDVIVK TPCPVVDDVK AQEIADKIYN LFNGYTSGKE QQTAYNTLLD LGSPTLHRVL
YHYNQHYESF GEFTWRCEDE LGPRKAGLIL SQLGDLSSWC NGLLQEPKIS LRRGSLKYLG
CRYSEIKPYG LDWSELSRDL RKTCEEQTLS VPYNDYGDSK DI
