GenomeNet

Database: UniProt
Entry: O75129
LinkDB: O75129
Original site: O75129 
ID   ASTN2_HUMAN             Reviewed;        1339 AA.
AC   O75129; A2A2T7; A2A2T9; Q52LQ2; Q5JVX8; Q5JVX9; Q5JVY1; Q5VXG8;
AC   Q5VZX6; Q8N6P8; Q8WV47; Q96FL4; Q9UHW6;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   13-FEB-2019, entry version 137.
DE   RecName: Full=Astrotactin-2;
DE   Flags: Precursor;
GN   Name=ASTN2; Synonyms=KIAA0634;
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 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.
RT   The complete sequences of 100 new cDNA clones from brain which can
RT   code for 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.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   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.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   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.,
RA   Rogers J., 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
RT   project: 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.,
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   [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
RT   perforin-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.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   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.,
RA   Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
RA   Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
RA   Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
RA   Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
RA   Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
RA   Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
RA   Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
RA   Futreal P.A.;
RT   "Exome sequencing identifies frequent mutation of the SWI/SNF complex
RT   gene PBRM1 in renal carcinoma.";
RL   Nature 469:539-542(2011).
CC   -!- FUNCTION: Mediates recycling of the neuronal cell adhesion
CC       molecule ASTN1 to the anterior pole of the cell membrane in
CC       migrating neurons. Promotes ASTN1 internalization and
CC       intracellular transport of endocytosed ASTN1 (By similarity).
CC       Selectively binds inositol-4,5-bisphosphate, inositol-3,4,5-
CC       trisphosphate and inositol-1,3,4,5-tetrakisphosphate, suggesting
CC       it is recruited to membranes that contain lipids with a
CC       phosphoinositide headgroup (Ref.6). {ECO:0000250|UniProtKB:Q80Z10,
CC       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};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q80Z10}.
CC       Perikaryon {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-
CC       coated 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
CC       the cell cortex, close to the anterior pole of migrating neurons.
CC       Detected 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         Note=No experimental confirmation available.;
CC       Name=6;
CC         IsoId=O75129-6; Sequence=VSP_028930, VSP_028937;
CC   -!- DOMAIN: The C-terminal region after the fibronectin type-III
CC       domain presents structural similarity to annexin domains and binds
CC       calcium 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=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=BAA31609.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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   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   UniGene; Hs.601562; -.
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   ProteinModelPortal; O75129; -.
DR   SMR; O75129; -.
DR   BioGrid; 116849; 4.
DR   IntAct; O75129; 1.
DR   MINT; O75129; -.
DR   STRING; 9606.ENSP00000354504; -.
DR   iPTMnet; O75129; -.
DR   PhosphoSitePlus; O75129; -.
DR   BioMuta; ASTN2; -.
DR   jPOST; O75129; -.
DR   PaxDb; O75129; -.
DR   PeptideAtlas; O75129; -.
DR   PRIDE; O75129; -.
DR   ProteomicsDB; 49788; -.
DR   ProteomicsDB; 49789; -. [O75129-2]
DR   ProteomicsDB; 49790; -. [O75129-3]
DR   ProteomicsDB; 49791; -. [O75129-4]
DR   ProteomicsDB; 49792; -. [O75129-6]
DR   Ensembl; ENST00000288520; ENSP00000288520; ENSG00000148219. [O75129-4]
DR   Ensembl; ENST00000313400; ENSP00000314038; ENSG00000148219. [O75129-1]
DR   Ensembl; ENST00000341734; ENSP00000339925; ENSG00000148219. [O75129-6]
DR   Ensembl; ENST00000361209; ENSP00000354504; ENSG00000148219. [O75129-2]
DR   GeneID; 23245; -.
DR   KEGG; hsa:23245; -.
DR   UCSC; uc004bjp.3; human. [O75129-1]
DR   CTD; 23245; -.
DR   DisGeNET; 23245; -.
DR   EuPathDB; HostDB:ENSG00000148219.16; -.
DR   GeneCards; ASTN2; -.
DR   HGNC; HGNC:17021; ASTN2.
DR   HPA; HPA027035; -.
DR   MIM; 612856; gene.
DR   neXtProt; NX_O75129; -.
DR   OpenTargets; ENSG00000148219; -.
DR   PharmGKB; PA25076; -.
DR   eggNOG; ENOG410IHIU; Eukaryota.
DR   eggNOG; ENOG4110VB2; LUCA.
DR   GeneTree; ENSGT00390000003140; -.
DR   HOVERGEN; HBG050597; -.
DR   InParanoid; O75129; -.
DR   OMA; KHLCVRS; -.
DR   OrthoDB; 39300at2759; -.
DR   PhylomeDB; O75129; -.
DR   TreeFam; TF332034; -.
DR   ChiTaRS; ASTN2; human.
DR   GenomeRNAi; 23245; -.
DR   PRO; PR:O75129; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   Bgee; ENSG00000148219; Expressed in 188 organ(s), highest expression level in testis.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR040510; ASTN_2_hairpin.
DR   InterPro; IPR026995; Astrotactin.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR020864; MACPF.
DR   PANTHER; PTHR16592; PTHR16592; 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   3D-structure; Alternative splicing; Calcium; Complete proteome;
KW   Cytoplasm; Cytoplasmic vesicle; Disulfide bond; EGF-like domain;
KW   Endosome; Glycoprotein; Membrane; Metal-binding; Polymorphism;
KW   Protein transport; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     49       {ECO:0000255}.
FT   CHAIN        50   1339       Astrotactin-2.
FT                                /FTId=PRO_0000308252.
FT   TOPO_DOM     50    206       Lumenal. {ECO:0000305}.
FT   TRANSMEM    207    227       Helical. {ECO:0000255}.
FT   TOPO_DOM    228    434       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    435    455       Helical. {ECO:0000255}.
FT   TOPO_DOM    456   1339       Lumenal. {ECO:0000305}.
FT   DOMAIN      510    550       EGF-like 1.
FT   DOMAIN      651    695       EGF-like 2.
FT   DOMAIN      699    751       EGF-like 3.
FT   DOMAIN     1065   1188       Fibronectin type-III.
FT   CARBOHYD    168    168       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    770    770       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|Ref.6}.
FT   CARBOHYD    783    783       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|Ref.6}.
FT   CARBOHYD   1020   1020       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    514    526       {ECO:0000250}.
FT   DISULFID    522    533       {ECO:0000250}.
FT   DISULFID    535    549       {ECO:0000250}.
FT   DISULFID    655    668       {ECO:0000250}.
FT   DISULFID    662    679       {ECO:0000250}.
FT   DISULFID    681    694       {ECO:0000250}.
FT   DISULFID    703    715       {ECO:0000250}.
FT   DISULFID    711    735       {ECO:0000250}.
FT   DISULFID    737    750       {ECO:0000250}.
FT   DISULFID    825    987       {ECO:0000269|Ref.6}.
FT   DISULFID    916    977       {ECO:0000269|Ref.6}.
FT   DISULFID    983    990       {ECO:0000269|Ref.6}.
FT   DISULFID   1036   1047       {ECO:0000269|Ref.6}.
FT   DISULFID   1049   1062       {ECO:0000269|Ref.6}.
FT   DISULFID   1136   1158       {ECO:0000269|Ref.6}.
FT   DISULFID   1190   1277       {ECO:0000269|Ref.6}.
FT   DISULFID   1298   1321       {ECO:0000269|Ref.6}.
FT   VAR_SEQ       1    948       Missing (in isoform 6).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_028930.
FT   VAR_SEQ       1    899       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_028931.
FT   VAR_SEQ     339    389       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:9734811,
FT                                ECO:0000303|Ref.4}.
FT                                /FTId=VSP_028932.
FT   VAR_SEQ     584    587       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_028933.
FT   VAR_SEQ     900    935       YGSHYIAEALYGSELTCIIHFPSKKVQQQLWLQYQK -> M
FT                                NTLLCKGMFCLLSWEADSRGRLGEYTLQPLSLQTE (in
FT                                isoform 4).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_028934.
FT   VAR_SEQ    1334   1339       GESKGR -> YLTLSKVSPF (in isoform 6).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_028937.
FT   VARIANT      70     70       V -> I (in dbSNP:rs16933591).
FT                                /FTId=VAR_036765.
FT   VARIANT     229    229       A -> V (found in a clear cell renal
FT                                carcinoma case; somatic mutation).
FT                                {ECO:0000269|PubMed:21248752}.
FT                                /FTId=VAR_064699.
FT   VARIANT     865    865       R -> H (in dbSNP:rs3818503).
FT                                /FTId=VAR_036766.
FT   VARIANT    1149   1149       V -> I (in dbSNP:rs16933591).
FT                                /FTId=VAR_036767.
FT   VARIANT    1293   1293       V -> L (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036768.
FT   MUTAGEN    1175   1175       R->T: Abolishes inositol-4,5-bisphosphate
FT                                binding. Strongly reduces affinity for
FT                                inositol-3,4,5-trisphosphate.
FT                                {ECO:0000269|Ref.6}.
FT   CONFLICT   1320   1320       T -> M (in Ref. 3; AAH29272).
FT                                {ECO:0000305}.
FT   TURN        777    779       {ECO:0000244|PDB:5J67}.
FT   STRAND      783    785       {ECO:0000244|PDB:5J67}.
FT   STRAND      805    807       {ECO:0000244|PDB:5J67}.
FT   STRAND      814    818       {ECO:0000244|PDB:5J67}.
FT   TURN        821    825       {ECO:0000244|PDB:5J67}.
FT   STRAND      826    829       {ECO:0000244|PDB:5J67}.
FT   HELIX       836    839       {ECO:0000244|PDB:5J67}.
FT   STRAND      840    843       {ECO:0000244|PDB:5J67}.
FT   TURN        847    849       {ECO:0000244|PDB:5J67}.
FT   STRAND      853    860       {ECO:0000244|PDB:5J67}.
FT   STRAND      864    868       {ECO:0000244|PDB:5J67}.
FT   HELIX       875    886       {ECO:0000244|PDB:5J67}.
FT   HELIX       890    900       {ECO:0000244|PDB:5J67}.
FT   STRAND      902    911       {ECO:0000244|PDB:5J67}.
FT   STRAND      913    921       {ECO:0000244|PDB:5J67}.
FT   HELIX       923    937       {ECO:0000244|PDB:5J67}.
FT   HELIX       951    961       {ECO:0000244|PDB:5J67}.
FT   TURN        962    964       {ECO:0000244|PDB:5J67}.
FT   TURN        969    972       {ECO:0000244|PDB:5J67}.
FT   STRAND      974    981       {ECO:0000244|PDB:5J67}.
FT   STRAND      984    986       {ECO:0000244|PDB:5J67}.
FT   STRAND      988    990       {ECO:0000244|PDB:5J67}.
FT   TURN        993    995       {ECO:0000244|PDB:5J67}.
FT   STRAND      997    999       {ECO:0000244|PDB:5J67}.
FT   STRAND     1003   1012       {ECO:0000244|PDB:5J67}.
FT   HELIX      1013   1016       {ECO:0000244|PDB:5J67}.
FT   HELIX      1020   1035       {ECO:0000244|PDB:5J67}.
FT   STRAND     1039   1043       {ECO:0000244|PDB:5J67}.
FT   STRAND     1046   1049       {ECO:0000244|PDB:5J67}.
FT   STRAND     1083   1088       {ECO:0000244|PDB:5J67}.
FT   STRAND     1093   1095       {ECO:0000244|PDB:5J67}.
FT   STRAND     1098   1108       {ECO:0000244|PDB:5J67}.
FT   STRAND     1110   1113       {ECO:0000244|PDB:5J67}.
FT   STRAND     1120   1123       {ECO:0000244|PDB:5J67}.
FT   HELIX      1124   1128       {ECO:0000244|PDB:5J67}.
FT   TURN       1134   1136       {ECO:0000244|PDB:5J67}.
FT   STRAND     1137   1143       {ECO:0000244|PDB:5J67}.
FT   STRAND     1145   1148       {ECO:0000244|PDB:5J67}.
FT   STRAND     1150   1156       {ECO:0000244|PDB:5J67}.
FT   STRAND     1164   1173       {ECO:0000244|PDB:5J67}.
FT   STRAND     1182   1187       {ECO:0000244|PDB:5J67}.
FT   HELIX      1195   1211       {ECO:0000244|PDB:5J67}.
FT   HELIX      1215   1227       {ECO:0000244|PDB:5J67}.
FT   HELIX      1230   1244       {ECO:0000244|PDB:5J67}.
FT   HELIX      1245   1247       {ECO:0000244|PDB:5J67}.
FT   HELIX      1250   1258       {ECO:0000244|PDB:5J67}.
FT   HELIX      1260   1271       {ECO:0000244|PDB:5J67}.
FT   HELIX      1275   1280       {ECO:0000244|PDB:5J67}.
FT   STRAND     1283   1302       {ECO:0000244|PDB:5J67}.
FT   HELIX      1314   1316       {ECO:0000244|PDB:5J67}.
FT   STRAND     1319   1337       {ECO:0000244|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
//
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