GenomeNet

Database: UniProt
Entry: O14525
LinkDB: O14525
Original site: O14525 
ID   ASTN1_HUMAN             Reviewed;        1302 AA.
AC   O14525; A5PL12; B4DHI9; E9PFR8; O60799; Q5W0V7; Q5W0V8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 3.
DT   10-APR-2019, entry version 167.
DE   RecName: Full=Astrotactin-1;
DE   Flags: Precursor;
GN   Name=ASTN1; Synonyms=ASTN, KIAA0289;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP   ARG-932 AND GLN-942.
RC   TISSUE=Brain;
RX   PubMed=9179496; DOI=10.1093/dnares/4.1.53;
RA   Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N.,
RA   Nomura N.;
RT   "Construction and characterization of human brain cDNA libraries
RT   suitable for analysis of cDNA clones encoding relatively large
RT   proteins.";
RL   DNA Res. 4:53-59(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS
RP   ARG-932 AND GLN-942.
RC   TISSUE=Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS
RP   ARG-932 AND GLN-942.
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: 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
CC       migration of granule cells during brain development and for normal
CC       cerebellum development. {ECO:0000250|UniProtKB:Q61137}.
CC   -!- SUBUNIT: Interacts with ASTN2; the interaction is not calcium-
CC       dependent. {ECO:0000250|UniProtKB:Q61137}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:Q61137}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q61137}. Perikaryon
CC       {ECO:0000250|UniProtKB:Q61137}. Endosome
CC       {ECO:0000250|UniProtKB:Q61137}. Cytoplasmic vesicle, clathrin-
CC       coated vesicle {ECO:0000250|UniProtKB:Q61137}. Note=Detected close
CC       to the anterior pole and at the base of the leading process in
CC       migrating neurons. Is internalized from the membrane via clathrin-
CC       coated vesicles and endosomes, and recycled to the anterior pole
CC       of the migrating cell. {ECO:0000250|UniProtKB:Q61137}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=2;
CC         IsoId=O14525-1; Sequence=Displayed;
CC         Note=No experimental confirmation available.;
CC       Name=1;
CC         IsoId=O14525-2; Sequence=VSP_001371;
CC       Name=3;
CC         IsoId=O14525-3; Sequence=VSP_001371, VSP_045069;
CC         Note=Ref.2 (BAG58151) sequence is in conflict in position:
CC         1216:R->RYQ. {ECO:0000305};
CC   -!- SIMILARITY: Belongs to the astrotactin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA22958.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; AB006627; BAA22958.1; ALT_INIT; mRNA.
DR   EMBL; AK295126; BAG58151.1; -; mRNA.
DR   EMBL; AL021398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL022145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL031290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL136983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471067; EAW91007.1; -; Genomic_DNA.
DR   EMBL; BC142697; AAI42698.1; -; mRNA.
DR   CCDS; CCDS1319.1; -. [O14525-2]
DR   CCDS; CCDS44280.1; -. [O14525-3]
DR   PIR; T00038; T00038.
DR   RefSeq; NP_996991.1; NM_207108.2. [O14525-3]
DR   RefSeq; XP_016856829.1; XM_017001340.1.
DR   UniGene; Hs.495897; -.
DR   ProteinModelPortal; O14525; -.
DR   SMR; O14525; -.
DR   IntAct; O14525; 2.
DR   STRING; 9606.ENSP00000354536; -.
DR   TCDB; 9.B.87.2.1; the selenoprotein p receptor (selp-receptor) family.
DR   iPTMnet; O14525; -.
DR   PhosphoSitePlus; O14525; -.
DR   BioMuta; ASTN1; -.
DR   PaxDb; O14525; -.
DR   PeptideAtlas; O14525; -.
DR   PRIDE; O14525; -.
DR   ProteomicsDB; 48071; -.
DR   ProteomicsDB; 48072; -. [O14525-2]
DR   Ensembl; ENST00000361833; ENSP00000354536; ENSG00000152092. [O14525-2]
DR   Ensembl; ENST00000424564; ENSP00000395041; ENSG00000152092. [O14525-3]
DR   GeneID; 460; -.
DR   KEGG; hsa:460; -.
DR   UCSC; uc001glc.5; human. [O14525-1]
DR   CTD; 460; -.
DR   DisGeNET; 460; -.
DR   EuPathDB; HostDB:ENSG00000152092.15; -.
DR   GeneCards; ASTN1; -.
DR   HGNC; HGNC:773; ASTN1.
DR   HPA; HPA074112; -.
DR   MIM; 600904; gene.
DR   neXtProt; NX_O14525; -.
DR   OpenTargets; ENSG00000152092; -.
DR   PharmGKB; PA162376961; -.
DR   eggNOG; ENOG410IHIU; Eukaryota.
DR   eggNOG; ENOG4110VB2; LUCA.
DR   GeneTree; ENSGT00390000003140; -.
DR   HOGENOM; HOG000034112; -.
DR   HOVERGEN; HBG050597; -.
DR   InParanoid; O14525; -.
DR   OMA; ALYNILM; -.
DR   OrthoDB; 39300at2759; -.
DR   PhylomeDB; O14525; -.
DR   TreeFam; TF332034; -.
DR   ChiTaRS; ASTN1; human.
DR   GenomeRNAi; 460; -.
DR   PRO; PR:O14525; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000152092; Expressed in 132 organ(s), highest expression level in entorhinal cortex.
DR   ExpressionAtlas; O14525; baseline and differential.
DR   Genevisible; O14525; HS.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0007158; P:neuron cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR   CDD; cd00063; FN3; 1.
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   SMART; SM00181; EGF; 3.
DR   SMART; SM00457; MACPF; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell adhesion; Cell membrane; Complete proteome;
KW   Cytoplasmic vesicle; Disulfide bond; EGF-like domain; Endosome;
KW   Glycoprotein; Membrane; Methylation; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22   1302       Astrotactin-1.
FT                                /FTId=PRO_0000007481.
FT   TOPO_DOM     22    153       Extracellular. {ECO:0000305}.
FT   TRANSMEM    154    174       Helical. {ECO:0000255}.
FT   TOPO_DOM    175    383       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    384    402       Helical. {ECO:0000255}.
FT   TOPO_DOM    403   1302       Extracellular.
FT                                {ECO:0000250|UniProtKB:O75129}.
FT   DOMAIN      459    507       EGF-like 1.
FT   DOMAIN      608    652       EGF-like 2.
FT   DOMAIN      656    708       EGF-like 3.
FT   DOMAIN     1030   1145       Fibronectin type-III.
FT   MOD_RES     227    227       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q61137}.
FT   MOD_RES     337    337       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:Q61137}.
FT   CARBOHYD    115    115       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    453    453       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    729    729       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    742    742       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    804    804       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    984    984       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    463    475       {ECO:0000250}.
FT   DISULFID    471    490       {ECO:0000250}.
FT   DISULFID    492    506       {ECO:0000250}.
FT   DISULFID    612    625       {ECO:0000250}.
FT   DISULFID    619    636       {ECO:0000250}.
FT   DISULFID    638    651       {ECO:0000250}.
FT   DISULFID    660    672       {ECO:0000250}.
FT   DISULFID    668    692       {ECO:0000250}.
FT   DISULFID    694    707       {ECO:0000250}.
FT   DISULFID    785    951       {ECO:0000250|UniProtKB:O75129}.
FT   DISULFID    876    941       {ECO:0000250|UniProtKB:O75129}.
FT   DISULFID    947    954       {ECO:0000250|UniProtKB:O75129}.
FT   DISULFID   1000   1011       {ECO:0000250|UniProtKB:O75129}.
FT   DISULFID   1013   1026       {ECO:0000250|UniProtKB:O75129}.
FT   DISULFID   1101   1121       {ECO:0000250|UniProtKB:O75129}.
FT   DISULFID   1153   1240       {ECO:0000250|UniProtKB:O75129}.
FT   DISULFID   1261   1284       {ECO:0000250|UniProtKB:O75129}.
FT   VAR_SEQ     480    487       Missing (in isoform 1 and isoform 3).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:9179496}.
FT                                /FTId=VSP_001371.
FT   VAR_SEQ    1225   1302       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_045069.
FT   VARIANT     932    932       H -> R (in dbSNP:rs2228956).
FT                                {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:9179496}.
FT                                /FTId=VAR_069030.
FT   VARIANT     942    942       H -> Q (in dbSNP:rs2281180).
FT                                {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:9179496}.
FT                                /FTId=VAR_069031.
FT   VARIANT    1270   1270       G -> R (in dbSNP:rs12118933).
FT                                /FTId=VAR_036764.
FT   VARIANT    1278   1278       R -> G (in dbSNP:rs12118933).
FT                                /FTId=VAR_055713.
FT   CONFLICT    439    439       D -> E (in Ref. 2; BAG58151).
FT                                {ECO:0000305}.
FT   CONFLICT    994    994       T -> I (in Ref. 2; BAG58151).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1302 AA;  144913 MW;  CA9EDDA6621C4F3B CRC64;
     MALAGLCALL 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 AFLNPEGDSG TEAENDPQLT
     FYTDPSRSRR RSRVGSPRSP VNKTTLTLIS ITSCVIGLVC SSHVNCPLVV 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 DDPTLYNILM FCGCIEDYKL GVDGRSCQLI TETCPEGSDC
     GESRELPMNQ TLFGEMFFGY NNHSKEVAAG QVLKGTFRQN NFARGLDQQL PDGLVVATVP
     LENQCLEEIS EPTPDPDFLT GMVNFSEVSG YPVLQHWKVR SVMYHIKLNQ VAISQALSNA
     LHSLDGATSR ADFVALLDQF GNHYIQEAIY GFEESCSIWY PNKQVQRRLW LEYEDISKGN
     SPSDESEERE RDPKVLTFPE YITSLSDSGT KHMAAGVRME CHSKGRCPSS CPLCHVTSSP
     DTPAEPVLLE VTKAAPIYEL VTNNQTQRLL QEATMSSLWC SGTGDVIEDW CRCDSTAFGA
     DGLPTCAPLP QPVLRLSTVH EPSSTLVVLE WEHSEPPIGV QIVDYLLRQE KVTDRMDHSK
     VETETVLSFV DDIISGAKSP CAMPSQVPDK QLTTISLIIR CLEPDTIYMF TLWGVDNTGR
     RSRPSDVIVK TPCPVVDDVK AQEIADKIYN LFNGYTSGKE QQTAYNTLLD LGSPTLHRVL
     YHYNQHYESF GEFTWRCEDE LGPRKAGLIL SQLGDLSSWC NGLLQEPKIS LRRSSLKYLG
     CRYSEIKPYG LDWAELSRDL RKTCEEQTLS IPYNDYGDSK EI
//
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