ASTN2_MOUSE
ID ASTN2_MOUSE Reviewed; 1352 AA.
AC Q80Z10; E9Q8T4; Q6A031; Q811X9; Q811Y0; Q811Y1; Q811Y2;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Astrotactin-2;
DE Flags: Precursor;
GN Name=Astn2; Synonyms=Kiaa0634;
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 MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
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. 11:205-218(2004).
RN [2]
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 [3]
RP IDENTIFICATION BY 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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH ASTN1, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, ALTERNATIVE SPLICING, AND IDENTIFICATION
RP OF ISOFORM 3.
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).
CC -!- FUNCTION: Mediates recycling of the neuronal cell adhesion molecule
CC ASTN1 to the anterior pole of the cell membrane in migrating neurons.
CC Promotes ASTN1 internalization and intracellular transport of
CC endocytosed ASTN1 (PubMed:20573900). Selectively binds inositol-4,5-
CC bisphosphate, inositol-3,4,5-trisphosphate and inositol-1,3,4,5-
CC tetrakisphosphate, suggesting it is recruited to membranes that contain
CC lipids with a phosphoinositide headgroup (By similarity).
CC {ECO:0000250|UniProtKB:O75129, ECO:0000269|PubMed:20573900}.
CC -!- SUBUNIT: Interacts with ASTN1; the interaction is not calcium-
CC dependent. {ECO:0000269|PubMed:20573900}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:20573900}; Multi-
CC pass membrane protein {ECO:0000305}. Perikaryon
CC {ECO:0000269|PubMed:20573900}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:20573900}. Early endosome
CC {ECO:0000269|PubMed:20573900}. Late endosome
CC {ECO:0000269|PubMed:20573900}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000305|PubMed:20573900}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:20573900}. Note=Integral membrane protein not
CC detected at the cell membrane. Detected in cytoplasmic vesicles in the
CC cell cortex, close to the anterior pole of migrating neurons. Detected
CC at the base of the leading process in migrating neurons.
CC {ECO:0000269|PubMed:20573900}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q80Z10-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80Z10-2; Sequence=VSP_028938;
CC Name=3; Synonyms=a {ECO:0000303|PubMed:20573900};
CC IsoId=Q80Z10-3; Sequence=VSP_058454;
CC -!- TISSUE SPECIFICITY: Detected in cerebellum granule neurons; not
CC detected in astroglia (at protein level). Detected primarily in
CC cerebellum, and at lower levels in brain cortex, olfactory bulb,
CC hindbrain and hippocampus dentate gyrus. Between 6 and 10 days after
CC birth, when granule cell migration occurs in the cerebellum, detected
CC in granule cell precursors in the external germinal layer, the
CC molecular layer, the internal granule layer and in Purkinje neurons.
CC Detected in postmitotic neurons in adult cerebellum.
CC {ECO:0000269|PubMed:20573900}.
CC -!- DEVELOPMENTAL STAGE: Detected at low levels in embryonic brain. Highly
CC expressed 6 and 10 days after birth, when granule cell migration occurs
CC in the cerebellum; expression in cerebellum is considerably higher than
CC in brain cortex. Expressed at lower levels in adult cerebellum.
CC {ECO:0000269|PubMed:20573900}.
CC -!- DOMAIN: The C-terminal region after the fibronectin type-III domain
CC presents structural similarity to annexin domains and binds calcium
CC ions. {ECO:0000250|UniProtKB:O75129}.
CC -!- SIMILARITY: Belongs to the astrotactin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32265.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK172987; BAD32265.1; ALT_INIT; mRNA.
DR EMBL; AL691438; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL691454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL691456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL691474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL691475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL713878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL837523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18268.1; -. [Q80Z10-3]
DR CCDS; CCDS18269.1; -. [Q80Z10-1]
DR RefSeq; NP_062387.2; NM_019514.3. [Q80Z10-3]
DR RefSeq; NP_996992.1; NM_207109.2. [Q80Z10-1]
DR RefSeq; XP_006538167.1; XM_006538104.3. [Q80Z10-2]
DR AlphaFoldDB; Q80Z10; -.
DR SMR; Q80Z10; -.
DR STRING; 10090.ENSMUSP00000065786; -.
DR GlyConnect; 2137; 1 N-Linked glycan (1 site).
DR GlyGen; Q80Z10; 3 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q80Z10; -.
DR PhosphoSitePlus; Q80Z10; -.
DR MaxQB; Q80Z10; -.
DR PaxDb; Q80Z10; -.
DR PRIDE; Q80Z10; -.
DR ProteomicsDB; 277259; -. [Q80Z10-1]
DR ProteomicsDB; 277260; -. [Q80Z10-2]
DR ProteomicsDB; 277261; -. [Q80Z10-3]
DR Antibodypedia; 15627; 123 antibodies from 20 providers.
DR Ensembl; ENSMUST00000068214; ENSMUSP00000065786; ENSMUSG00000028373. [Q80Z10-1]
DR Ensembl; ENSMUST00000084496; ENSMUSP00000081540; ENSMUSG00000028373. [Q80Z10-3]
DR GeneID; 56079; -.
DR KEGG; mmu:56079; -.
DR UCSC; uc008thn.1; mouse. [Q80Z10-1]
DR UCSC; uc008tho.1; mouse.
DR UCSC; uc008thp.1; mouse. [Q80Z10-2]
DR CTD; 23245; -.
DR MGI; MGI:1889277; Astn2.
DR VEuPathDB; HostDB:ENSMUSG00000028373; -.
DR eggNOG; ENOG502R4QT; Eukaryota.
DR GeneTree; ENSGT00390000003140; -.
DR InParanoid; Q80Z10; -.
DR OMA; CHEGFAP; -.
DR OrthoDB; 39300at2759; -.
DR PhylomeDB; Q80Z10; -.
DR TreeFam; TF332034; -.
DR BioGRID-ORCS; 56079; 4 hits in 43 CRISPR screens.
DR ChiTaRS; Astn2; mouse.
DR PRO; PR:Q80Z10; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q80Z10; protein.
DR Bgee; ENSMUSG00000028373; Expressed in neural tube mantle layer and 83 other tissues.
DR Genevisible; Q80Z10; MM.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0060187; C:cell pole; IDA:MGI.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0043533; F:inositol 1,3,4,5 tetrakisphosphate binding; ISS:UniProtKB.
DR GO; GO:0048105; P:establishment of body hair planar orientation; IGI:MGI.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; IDA:MGI.
DR GO; GO:0007158; P:neuron cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; IBA:GO_Central.
DR GO; GO:0034394; P:protein localization to cell surface; IDA:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; IPR040510; ASTN_2_hairpin.
DR InterPro; IPR026995; Astrotactin.
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 Pfam; PF18577; ASTN_2_hairpin; 1.
DR Pfam; PF01823; MACPF; 1.
DR SMART; SM00457; MACPF; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cytoplasm; Cytoplasmic vesicle;
KW Disulfide bond; EGF-like domain; Endosome; Glycoprotein; Membrane;
KW Metal-binding; Protein transport; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..51
FT /evidence="ECO:0000255"
FT CHAIN 52..1352
FT /note="Astrotactin-2"
FT /id="PRO_0000308253"
FT TOPO_DOM 52..218
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..1352
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:20573900"
FT DOMAIN 523..563
FT /note="EGF-like 1"
FT DOMAIN 664..708
FT /note="EGF-like 2"
FT DOMAIN 712..764
FT /note="EGF-like 3"
FT DOMAIN 1079..1201
FT /note="Fibronectin type-III"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 796
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1033
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 527..539
FT /evidence="ECO:0000250"
FT DISULFID 535..546
FT /evidence="ECO:0000250"
FT DISULFID 548..562
FT /evidence="ECO:0000250"
FT DISULFID 668..681
FT /evidence="ECO:0000250"
FT DISULFID 675..692
FT /evidence="ECO:0000250"
FT DISULFID 694..707
FT /evidence="ECO:0000250"
FT DISULFID 716..728
FT /evidence="ECO:0000250"
FT DISULFID 724..748
FT /evidence="ECO:0000250"
FT DISULFID 750..763
FT /evidence="ECO:0000250"
FT DISULFID 838..1000
FT /evidence="ECO:0000250|UniProtKB:O75129"
FT DISULFID 929..990
FT /evidence="ECO:0000250|UniProtKB:O75129"
FT DISULFID 996..1003
FT /evidence="ECO:0000250|UniProtKB:O75129"
FT DISULFID 1049..1060
FT /evidence="ECO:0000250|UniProtKB:O75129"
FT DISULFID 1062..1075
FT /evidence="ECO:0000250|UniProtKB:O75129"
FT DISULFID 1149..1171
FT /evidence="ECO:0000250|UniProtKB:O75129"
FT DISULFID 1203..1290
FT /evidence="ECO:0000250|UniProtKB:O75129"
FT DISULFID 1311..1334
FT /evidence="ECO:0000250|UniProtKB:O75129"
FT VAR_SEQ 351..402
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:20573900, ECO:0000305"
FT /id="VSP_058454"
FT VAR_SEQ 597..600
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_028938"
SQ SEQUENCE 1352 AA; 149390 MW; 76D88651761FB04B CRC64;
MAAAGARRSP GRGLGLRGRP RLGFHPGPPP PPPPPLLLLF LLLLPPPPLL AGATAAAASR
EPDSPCRLKT VTVSTLPALR ESDIGWSGAR TGAAAGAGAG TGAGAGAAAA AASAASPGSA
GSAGTAAESR LLLFVRNELP GRIAVQDDLD NTELPFFTLE MSGTAADISL VHWRQQWLEN
GTLYFHVSMS SSGQLAQATA PTLQEPSEIV EEQMHILHIS VMGGLIALLL LLLVFTVALY
AQRRWQKRRR IPQKSASTEA THEIHYIPSV LLGPQARESF RSSRLQTHNS VIGVPIRETP
ILDDYDYEEE EEPPRRANHV SREDEFGSQM THALDSLGRP GEEKVEFEKK AAAEATQETV
ESLMQKFKES FRANTPVEIG QLQPASRSST SAGKRKRRNK SRGGISFGRT KGTSGSEADD
ETQLTFYTEQ YRSRRRSKGL LKSPVNKTAL TLIAVSSCIL AMVCGNQMSC PLTVKVTLHV
PEHFIADGSS FVVSEGSYLD ISDWLNPAKL SLYYQINATS PWVRDLCGQR TTDACEQLCD
PDTGECSCHE GYAPDPVHRH LCVRSDWGQS EGPWPYTTLE RGYDLVTGEQ APEKILRSTF
SLGQGLWLPV SKSFVVPPVE LSINPLASCK TDVLVTEDPA DVREEAMLST YFETINDLLS
SFGPVRDCSR NNGGCTRNFK CVSDRQVDSS GCVCPEELKP MKDGSGCYDH SKGIDCSDGF
NGGCEQLCLQ QTLPLPYDTT SSTIFMFCGC VEEYKLAPDG KSCLMLSDVC EGPKCLKPDS
KFNDTLFGEM LHGYNNRTQH VNQGQVFQMT FRENNFIKDF PQLADGLLVI PLPVEEQCRG
VLSEPLPDLQ LLTGDIRYDE AMGYPMVQQW RVRSNLYRVK LSTITLSAGF TNVLKILTKE
SSRDELLSFI QHYGSHYIAE ALYGSELTCI IHFPSKKVQQ QLWLQYQKET TELGSKKELK
SMPFITYLSG LLTAQMLSDD QLISGVEIRC EEKGRCPSTC HLCRRPGKEQ LSPTPVLLEI
NRVVPLYTLI QDNGTKEAFK NALMSSYWCS GKGDVIDDWC RCDLSAFDAS GLPNCSPLPQ
PVLRLSPTVE PSSTVVSLEW VDVQPAIGTK VSDYILQHKK VDEYTDTDLY TGEFLSFADD
LLSGLGTSCV AAGRSHGEVP EVSIYSVIFK CLEPDGLYKF TLYAVDTRGR HSELSTVTLR
TACPLVDDNK AEEIADKIYN LYNGYTSGKE QQTAYNTLME VSASMLFRVQ HHYNSHYEKF
GDFVWRSEDE LGPRKAHLIL RRLERVSSHC SSLLRSAYIQ SRVDTIPYLF CRSEEVRPAG
MVWYSILKDT KITCEEKMVS MARNTYGETK GR
