ID ASTN2_HUMAN Reviewed; 1339 AA.
AC O75129; A2A2T7; A2A2T9; Q52LQ2; Q5JVX8; Q5JVX9; Q5JVY1; Q5VXG8; Q5VZX6;
AC Q8N6P8; Q8WV47; Q96FL4; Q9UHW6;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 24-JAN-2024, entry version 162.
DE RecName: Full=Astrotactin-2;
DE Flags: Precursor;
GN Name=ASTN2; Synonyms=KIAA0634;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 6), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 532-1339 (ISOFORM 3).
RC TISSUE=Brain, Cervix, and Eye;
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 227-1339 (ISOFORM 2).
RC TISSUE=Uterus;
RA Tomoda T.;
RT "Molecular cloning of human astrotactin-2.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 274-470 (ISOFORM 1).
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [6]
RP X-RAY CRYSTALLOGRAPHY (3.16 ANGSTROMS) OF 768-1339, DISULFIDE BONDS,
RP GLYCOSYLATION AT ASN-770 AND ASN-783, CALCIUM-BINDING, FUNCTION,
RP MUTAGENESIS OF ARG-1175, AND DOMAIN.
RX DOI=10.1098/RSOB.160053;
RA Ni T., Harlos K., Gilbert R.;
RT "Structure of astrotactin-2: a conserved vertebrate-specific and perforin-
RT like membrane protein involved in neuronal development.";
RL Open Biol. 0:0-0(2016).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-1293.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [8]
RP VARIANT VAL-229.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
RN [9]
RP VARIANT HIS-298.
RX PubMed=28940097; DOI=10.1007/s00439-017-1843-2;
RA Anazi S., Maddirevula S., Salpietro V., Asi Y.T., Alsahli S., Alhashem A.,
RA Shamseldin H.E., AlZahrani F., Patel N., Ibrahim N., Abdulwahab F.M.,
RA Hashem M., Alhashmi N., Al Murshedi F., Al Kindy A., Alshaer A.,
RA Rumayyan A., Al Tala S., Kurdi W., Alsaman A., Alasmari A., Banu S.,
RA Sultan T., Saleh M.M., Alkuraya H., Salih M.A., Aldhalaan H., Ben-Omran T.,
RA Al Musafri F., Ali R., Suleiman J., Tabarki B., El-Hattab A.W., Bupp C.,
RA Alfadhel M., Al Tassan N., Monies D., Arold S.T., Abouelhoda M.,
RA Lashley T., Houlden H., Faqeih E., Alkuraya F.S.;
RT "Expanding the genetic heterogeneity of intellectual disability.";
RL Hum. Genet. 136:1419-1429(2017).
RN [10]
RP ERRATUM OF PUBMED:28940097.
RX PubMed=29288388; DOI=10.1007/s00439-017-1859-7;
RA Anazi S., Maddirevula S., Salpietro V., Asi Y.T., Alsahli S., Alhashem A.,
RA Shamseldin H.E., AlZahrani F., Patel N., Ibrahim N., Abdulwahab F.M.,
RA Hashem M., Alhashmi N., Al Murshedi F., Al Kindy A., Alshaer A.,
RA Rumayyan A., Al Tala S., Kurdi W., Alsaman A., Alasmari A., Banu S.,
RA Sultan T., Saleh M.M., Alkuraya H., Salih M.A., Aldhalaan H., Ben-Omran T.,
RA Al Musafri F., Ali R., Suleiman J., Tabarki B., El-Hattab A.W., Bupp C.,
RA Alfadhel M., Al Tassan N., Monies D., Arold S.T., Abouelhoda M.,
RA Lashley T., Houlden H., Faqeih E., Alkuraya F.S.;
RT "Correction to: Expanding the genetic heterogeneity of intellectual
RT disability.";
RL Hum. Genet. 137:105-109(2018).
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 (By similarity). 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 (Ref.6).
CC {ECO:0000250|UniProtKB:Q80Z10, ECO:0000269|Ref.6}.
CC -!- SUBUNIT: Interacts with ASTN1; the interaction is not calcium-
CC dependent. {ECO:0000250|UniProtKB:Q80Z10}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q80Z10}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:Q80Z10}. Perikaryon
CC {ECO:0000250|UniProtKB:Q80Z10}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q80Z10}. Early endosome
CC {ECO:0000250|UniProtKB:Q80Z10}. Late endosome
CC {ECO:0000250|UniProtKB:Q80Z10}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000250|UniProtKB:Q80Z10}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q80Z10}. 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:0000250|UniProtKB:Q80Z10}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=O75129-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75129-2; Sequence=VSP_028932;
CC Name=3;
CC IsoId=O75129-3; Sequence=VSP_028933;
CC Name=4;
CC IsoId=O75129-4; Sequence=VSP_028931, VSP_028934;
CC Name=6;
CC IsoId=O75129-6; Sequence=VSP_028930, VSP_028937;
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:0000269|Ref.6}.
CC -!- SIMILARITY: Belongs to the astrotactin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF14357.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA31609.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB014534; BAA31609.1; ALT_INIT; mRNA.
DR EMBL; AL133282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354981; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL392085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018759; AAH18759.2; -; mRNA.
DR EMBL; BC029272; AAH29272.1; -; mRNA.
DR EMBL; BC093835; AAH93835.2; -; mRNA.
DR EMBL; BC101667; AAI01668.1; -; mRNA.
DR EMBL; BC146756; AAI46757.1; -; mRNA.
DR EMBL; AF116574; AAF14357.1; ALT_INIT; mRNA.
DR EMBL; DA336442; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS48009.2; -. [O75129-4]
DR CCDS; CCDS6814.1; -. [O75129-6]
DR CCDS; CCDS6815.1; -. [O75129-2]
DR CCDS; CCDS6816.1; -. [O75129-1]
DR PIR; T00382; T00382.
DR RefSeq; NP_054729.3; NM_014010.4. [O75129-2]
DR RefSeq; NP_937829.3; NM_198186.3. [O75129-4]
DR RefSeq; NP_937831.1; NM_198188.2. [O75129-6]
DR PDB; 5J67; X-ray; 3.16 A; A/B/C/D=768-1339.
DR PDB; 5J68; X-ray; 5.22 A; A=768-1339.
DR PDB; 5J69; X-ray; 3.63 A; A/B=768-1033.
DR PDBsum; 5J67; -.
DR PDBsum; 5J68; -.
DR PDBsum; 5J69; -.
DR AlphaFoldDB; O75129; -.
DR SMR; O75129; -.
DR BioGRID; 116849; 11.
DR IntAct; O75129; 3.
DR MINT; O75129; -.
DR STRING; 9606.ENSP00000354504; -.
DR GlyCosmos; O75129; 4 sites, No reported glycans.
DR GlyGen; O75129; 8 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O75129; -.
DR PhosphoSitePlus; O75129; -.
DR BioMuta; ASTN2; -.
DR jPOST; O75129; -.
DR MassIVE; O75129; -.
DR PaxDb; 9606-ENSP00000354504; -.
DR PeptideAtlas; O75129; -.
DR ProteomicsDB; 49788; -. [O75129-1]
DR ProteomicsDB; 49789; -. [O75129-2]
DR ProteomicsDB; 49790; -. [O75129-3]
DR ProteomicsDB; 49791; -. [O75129-4]
DR ProteomicsDB; 49792; -. [O75129-6]
DR Antibodypedia; 15627; 138 antibodies from 22 providers.
DR DNASU; 23245; -.
DR Ensembl; ENST00000288520.9; ENSP00000288520.5; ENSG00000148219.18. [O75129-4]
DR Ensembl; ENST00000313400.9; ENSP00000314038.4; ENSG00000148219.18. [O75129-1]
DR Ensembl; ENST00000341734.8; ENSP00000339925.4; ENSG00000148219.18. [O75129-6]
DR Ensembl; ENST00000361209.6; ENSP00000354504.2; ENSG00000148219.18. [O75129-2]
DR GeneID; 23245; -.
DR KEGG; hsa:23245; -.
DR MANE-Select; ENST00000313400.9; ENSP00000314038.4; NM_001365068.1; NP_001351997.1.
DR UCSC; uc004bjp.3; human. [O75129-1]
DR AGR; HGNC:17021; -.
DR CTD; 23245; -.
DR DisGeNET; 23245; -.
DR GeneCards; ASTN2; -.
DR HGNC; HGNC:17021; ASTN2.
DR HPA; ENSG00000148219; Low tissue specificity.
DR MalaCards; ASTN2; -.
DR MIM; 612856; gene.
DR neXtProt; NX_O75129; -.
DR OpenTargets; ENSG00000148219; -.
DR PharmGKB; PA25076; -.
DR VEuPathDB; HostDB:ENSG00000148219; -.
DR eggNOG; ENOG502R4QT; Eukaryota.
DR GeneTree; ENSGT00390000003140; -.
DR HOGENOM; CLU_057342_0_0_1; -.
DR InParanoid; O75129; -.
DR OMA; CHEGFAP; -.
DR OrthoDB; 4157619at2759; -.
DR PhylomeDB; O75129; -.
DR TreeFam; TF332034; -.
DR PathwayCommons; O75129; -.
DR SignaLink; O75129; -.
DR SIGNOR; O75129; -.
DR BioGRID-ORCS; 23245; 13 hits in 1147 CRISPR screens.
DR ChiTaRS; ASTN2; human.
DR GenomeRNAi; 23245; -.
DR Pharos; O75129; Tbio.
DR PRO; PR:O75129; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O75129; Protein.
DR Bgee; ENSG00000148219; Expressed in buccal mucosa cell and 162 other cell types or tissues.
DR ExpressionAtlas; O75129; baseline and differential.
DR Genevisible; O75129; HS.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0060187; C:cell pole; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0043533; F:inositol 1,3,4,5 tetrakisphosphate binding; IDA:UniProtKB.
DR GO; GO:0048105; P:establishment of body hair planar orientation; IEA:Ensembl.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR040685; Annexin-like.
DR InterPro; IPR045574; ASTN1_2_Fn3.
DR InterPro; IPR045575; ASTN_1_2_N.
DR InterPro; IPR040510; ASTN_2_hairpin.
DR InterPro; IPR026995; Astrotactin.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR020864; MACPF.
DR PANTHER; PTHR16592; -; 1.
DR PANTHER; PTHR16592:SF2; ASTROTACTIN-2; 1.
DR Pfam; PF18411; Annexin_2; 1.
DR Pfam; PF19743; ASTN1_2_fn3; 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; Fibronectin type III; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cytoplasm;
KW Cytoplasmic vesicle; Disulfide bond; EGF-like domain; Endosome;
KW Glycoprotein; Membrane; Metal-binding; Protein transport;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..49
FT /evidence="ECO:0000255"
FT CHAIN 50..1339
FT /note="Astrotactin-2"
FT /id="PRO_0000308252"
FT TOPO_DOM 50..206
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..434
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..1339
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 510..550
FT /note="EGF-like 1"
FT DOMAIN 651..695
FT /note="EGF-like 2"
FT DOMAIN 699..751
FT /note="EGF-like 3"
FT DOMAIN 1065..1188
FT /note="Fibronectin type-III"
FT REGION 296..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 770
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.6"
FT CARBOHYD 783
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.6"
FT CARBOHYD 1020
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 514..526
FT /evidence="ECO:0000250"
FT DISULFID 522..533
FT /evidence="ECO:0000250"
FT DISULFID 535..549
FT /evidence="ECO:0000250"
FT DISULFID 655..668
FT /evidence="ECO:0000250"
FT DISULFID 662..679
FT /evidence="ECO:0000250"
FT DISULFID 681..694
FT /evidence="ECO:0000250"
FT DISULFID 703..715
FT /evidence="ECO:0000250"
FT DISULFID 711..735
FT /evidence="ECO:0000250"
FT DISULFID 737..750
FT /evidence="ECO:0000250"
FT DISULFID 825..987
FT /evidence="ECO:0000269|Ref.6"
FT DISULFID 916..977
FT /evidence="ECO:0000269|Ref.6"
FT DISULFID 983..990
FT /evidence="ECO:0000269|Ref.6"
FT DISULFID 1036..1047
FT /evidence="ECO:0000269|Ref.6"
FT DISULFID 1049..1062
FT /evidence="ECO:0000269|Ref.6"
FT DISULFID 1136..1158
FT /evidence="ECO:0000269|Ref.6"
FT DISULFID 1190..1277
FT /evidence="ECO:0000269|Ref.6"
FT DISULFID 1298..1321
FT /evidence="ECO:0000269|Ref.6"
FT VAR_SEQ 1..948
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028930"
FT VAR_SEQ 1..899
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028931"
FT VAR_SEQ 339..389
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9734811, ECO:0000303|Ref.4"
FT /id="VSP_028932"
FT VAR_SEQ 584..587
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028933"
FT VAR_SEQ 900..935
FT /note="YGSHYIAEALYGSELTCIIHFPSKKVQQQLWLQYQK -> MNTLLCKGMFCL
FT LSWEADSRGRLGEYTLQPLSLQTE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028934"
FT VAR_SEQ 1334..1339
FT /note="GESKGR -> YLTLSKVSPF (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028937"
FT VARIANT 70
FT /note="V -> I (in dbSNP:rs16933591)"
FT /id="VAR_036765"
FT VARIANT 229
FT /note="A -> V (found in a clear cell renal carcinoma case;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064699"
FT VARIANT 298
FT /note="D -> H (found in a patient with global developmental
FT delay; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:28940097"
FT /id="VAR_084650"
FT VARIANT 865
FT /note="R -> H (in dbSNP:rs3818503)"
FT /id="VAR_036766"
FT VARIANT 1149
FT /note="V -> I (in dbSNP:rs16933591)"
FT /id="VAR_036767"
FT VARIANT 1293
FT /note="V -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036768"
FT MUTAGEN 1175
FT /note="R->T: Abolishes inositol-4,5-bisphosphate binding.
FT Strongly reduces affinity for inositol-3,4,5-
FT trisphosphate."
FT /evidence="ECO:0000269|Ref.6"
FT CONFLICT 1320
FT /note="T -> M (in Ref. 3; AAH29272)"
FT /evidence="ECO:0000305"
FT TURN 777..779
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 783..785
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 805..807
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 814..818
FT /evidence="ECO:0007829|PDB:5J67"
FT TURN 821..825
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 826..829
FT /evidence="ECO:0007829|PDB:5J67"
FT HELIX 836..839
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 840..843
FT /evidence="ECO:0007829|PDB:5J67"
FT TURN 847..849
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 853..860
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 864..868
FT /evidence="ECO:0007829|PDB:5J67"
FT HELIX 875..886
FT /evidence="ECO:0007829|PDB:5J67"
FT HELIX 890..900
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 902..911
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 913..921
FT /evidence="ECO:0007829|PDB:5J67"
FT HELIX 923..937
FT /evidence="ECO:0007829|PDB:5J67"
FT HELIX 951..961
FT /evidence="ECO:0007829|PDB:5J67"
FT TURN 962..964
FT /evidence="ECO:0007829|PDB:5J67"
FT TURN 969..972
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 974..981
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 984..986
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 988..990
FT /evidence="ECO:0007829|PDB:5J67"
FT TURN 993..995
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 997..999
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 1003..1012
FT /evidence="ECO:0007829|PDB:5J67"
FT HELIX 1013..1016
FT /evidence="ECO:0007829|PDB:5J67"
FT HELIX 1020..1035
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 1039..1043
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 1046..1049
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 1083..1088
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 1093..1095
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 1098..1108
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 1110..1113
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 1120..1123
FT /evidence="ECO:0007829|PDB:5J67"
FT HELIX 1124..1128
FT /evidence="ECO:0007829|PDB:5J67"
FT TURN 1134..1136
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 1137..1143
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 1145..1148
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 1150..1156
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 1164..1173
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 1182..1187
FT /evidence="ECO:0007829|PDB:5J67"
FT HELIX 1195..1211
FT /evidence="ECO:0007829|PDB:5J67"
FT HELIX 1215..1227
FT /evidence="ECO:0007829|PDB:5J67"
FT HELIX 1230..1244
FT /evidence="ECO:0007829|PDB:5J67"
FT HELIX 1245..1247
FT /evidence="ECO:0007829|PDB:5J67"
FT HELIX 1250..1258
FT /evidence="ECO:0007829|PDB:5J67"
FT HELIX 1260..1271
FT /evidence="ECO:0007829|PDB:5J67"
FT HELIX 1275..1280
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 1283..1302
FT /evidence="ECO:0007829|PDB:5J67"
FT HELIX 1314..1316
FT /evidence="ECO:0007829|PDB:5J67"
FT STRAND 1319..1337
FT /evidence="ECO:0007829|PDB:5J67"
SQ SEQUENCE 1339 AA; 148243 MW; 7B914F1A736F798F CRC64;
MAAAGARLSP GPGSGLRGRP RLCFHPGPPP LLPLLLLFLL LLPPPPLLAG ATAAASREPD
SPCRLKTVTV STLPALRESD IGWSGARAGA GAGTGAGAAA AAASPGSPGS AGTAAESRLL
LFVRNELPGR IAVQDDLDNT ELPFFTLEMS GTAADISLVH WRQQWLENGT LYFHVSMSSS
GQLAQATAPT LQEPSEIVEE QMHILHISVM GGLIALLLLL LVFTVALYAQ RRWQKRRRIP
QKSASTEATH EIHYIPSVLL GPQARESFRS SRLQTHNSVI GVPIRETPIL DDYDCEEDEE
PPRRANHVSR EDEFGSQVTH TLDSLGHPGE EKVDFEKKAA AEATQETVES LMQKFKESFR
ANTPIEIGQL QPPLRSTSAG KRKRRSKSRG GISFGRAKGT SGSEADDETQ LTFYTEQYRS
RRRSKGLLKS PVNKTALTLI AVSSCILAMV CGSQMSCPLT VKVTLHVPEH FIADGSSFVV
SEGSYLDISD WLNPAKLSLY YQINATSPWV RDLCGQRTTD ACEQLCDPET GECSCHEGYA
PDPVHRHLCV RSDWGQSEGP WPYTTLERGY DLVTGEQAPE KILRSTFSLG QGLWLPVSKS
FVVPPVELSI NPLASCKTDV LVTEDPADVR EEAMLSTYFE TINDLLSSFG PVRDCSRNNG
GCTRNFKCVS DRQVDSSGCV CPEELKPMKD GSGCYDHSKG IDCSDGFNGG CEQLCLQQTL
PLPYDATSST IFMFCGCVEE YKLAPDGKSC LMLSDVCEGP KCLKPDSKFN DTLFGEMLHG
YNNRTQHVNQ GQVFQMTFRE NNFIKDFPQL ADGLLVIPLP VEEQCRGVLS EPLPDLQLLT
GDIRYDEAMG YPMVQQWRVR SNLYRVKLST ITLAAGFTNV LKILTKESSR EELLSFIQHY
GSHYIAEALY GSELTCIIHF PSKKVQQQLW LQYQKETTEL GSKKELKSMP FITYLSGLLT
AQMLSDDQLI SGVEIRCEEK GRCPSTCHLC RRPGKEQLSP TPVLLEINRV VPLYTLIQDN
GTKEAFKSAL MSSYWCSGKG DVIDDWCRCD LSAFDANGLP NCSPLLQPVL RLSPTVEPSS
TVVSLEWVDV QPAIGTKVSD YILQHKKVDE YTDTDLYTGE FLSFADDLLS GLGTSCVAAG
RSHGEVPEVS IYSVIFKCLE PDGLYKFTLY AVDTRGRHSE LSTVTLRTAC PLVDDNKAEE
IADKIYNLYN GYTSGKEQQM AYNTLMEVSA SMLFRVQHHY NSHYEKFGDF VWRSEDELGP
RKAHLILRRL ERVSSHCSSL LRSAYIQSRV ETVPYLFCRS EEVRPAGMVW YSILKDTKIT
CEEKMVSMAR NTYGESKGR
//
