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}; 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; 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 //