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 13-FEB-2019, entry version 166. 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}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- 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 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 //