ID ASPC1_HUMAN Reviewed; 553 AA. AC Q9BZE9; A8K3K9; Q7Z6N7; Q8WV59; Q96LS5; Q96M40; DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 164. DE RecName: Full=Tether containing UBX domain for GLUT4; DE AltName: Full=Alveolar soft part sarcoma chromosomal region candidate gene 1 protein; DE AltName: Full=Alveolar soft part sarcoma locus; DE AltName: Full=Renal papillary cell carcinoma protein 17; DE AltName: Full=UBX domain-containing protein 9; GN Name=ASPSCR1; Synonyms=ASPL, RCC17, TUG, UBXD9, UBXN9; 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 [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION WITH RP TFE3, TISSUE SPECIFICITY, AND INVOLVEMENT IN ASPS. RX PubMed=11244503; DOI=10.1038/sj.onc.1204074; RA Ladanyi M., Lui M.Y., Antonescu C.R., Krause-Boehm A., Meindl A., RA Argani P., Healey J.H., Ueda T., Yoshikawa H., Meloni-Ehrig A., RA Sorensen P.H.B., Mertens F., Mandahl N., van den Berghe H., Sciot R., RA Dal Cin P., Bridge J.; RT "The der(17)t(X;17)(p11;q25) of human alveolar soft part sarcoma fuses the RT TFE3 transcription factor gene to ASPL, a novel gene at 17q25."; RL Oncogene 20:48-57(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT RP GLN-252. RC TISSUE=Brain, Heart, and Testis; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT RP GLN-252. RC TISSUE=Eye, and Skin; 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 CHROMOSOMAL TRANSLOCATION WITH TFE3, AND TISSUE SPECIFICITY. RX PubMed=11358836; RA Heimann P., El Housni H., Ogur G., Weterman M.A.J., Petty E.M., Vassart G.; RT "Fusion of a novel gene, RCC17, to the TFE3 gene in t(X;17)(p11.2;q25.3)- RT bearing papillary renal cell carcinomas."; RL Cancer Res. 61:4130-4135(2001). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [8] RP SUBCELLULAR LOCATION, AND INTERACTION WITH VCP. RX PubMed=22207755; DOI=10.1074/jbc.m111.284232; RA Orme C.M., Bogan J.S.; RT "The ubiquitin regulatory X (UBX) domain-containing protein TUG regulates RT the p97 ATPase and resides at the endoplasmic reticulum-golgi intermediate RT compartment."; RL J. Biol. Chem. 287:6679-6692(2012). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-500 AND SER-502, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] RP FUNCTION IN VCP METHYLATION, INTERACTION WITH VCPKMT, AND SUBCELLULAR RP LOCATION. RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210; RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.; RT "A newly uncovered group of distantly related lysine methyltransferases RT preferentially interact with molecular chaperones to regulate their RT activity."; RL PLoS Genet. 9:E1003210-E1003210(2013). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-500 AND SER-502, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Tethering protein that sequesters GLUT4-containing vesicles CC in the cytoplasm in the absence of insulin. Modulates the amount of CC GLUT4 that is available at the cell surface (By similarity). Enhances CC VCP methylation catalyzed by VCPKMT. {ECO:0000250, CC ECO:0000269|PubMed:23349634}. CC -!- SUBUNIT: Interacts with GLUT4 (By similarity). Interacts with VCPKMT. CC Interacts with VCP. {ECO:0000250, ECO:0000269|PubMed:22207755, CC ECO:0000269|PubMed:23349634}. CC -!- INTERACTION: CC Q9BZE9; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-1993677, EBI-10173507; CC Q9BZE9; P49760: CLK2; NbExp=3; IntAct=EBI-1993677, EBI-750020; CC Q9BZE9; Q0VD86: INCA1; NbExp=3; IntAct=EBI-1993677, EBI-6509505; CC Q9BZE9; Q15323: KRT31; NbExp=3; IntAct=EBI-1993677, EBI-948001; CC Q9BZE9; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-1993677, EBI-11959885; CC Q9BZE9; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-1993677, EBI-10171774; CC Q9BZE9; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-1993677, EBI-945833; CC Q9BZE9; Q9Y6A5: TACC3; NbExp=3; IntAct=EBI-1993677, EBI-2554984; CC Q9BZE9; P15884: TCF4; NbExp=3; IntAct=EBI-1993677, EBI-533224; CC Q9BZE9; P55072: VCP; NbExp=31; IntAct=EBI-1993677, EBI-355164; CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral CC membrane protein {ECO:0000250}. Endoplasmic reticulum-Golgi CC intermediate compartment membrane {ECO:0000269|PubMed:22207755}; CC Peripheral membrane protein. Cytoplasm {ECO:0000269|PubMed:23349634}. CC Nucleus {ECO:0000269|PubMed:23349634}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9BZE9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BZE9-2; Sequence=VSP_020578; CC Name=3; CC IsoId=Q9BZE9-3; Sequence=VSP_020574, VSP_020577; CC Name=4; CC IsoId=Q9BZE9-4; Sequence=VSP_020574, VSP_020575, VSP_020576; CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in testis, heart, CC skeletal muscle and pancreas. {ECO:0000269|PubMed:11244503, CC ECO:0000269|PubMed:11358836}. CC -!- DISEASE: Note=A chromosomal aberration involving ASPSCR1 is found in CC patients with alveolar soft part sarcoma. Translocation CC t(X;17)(p11;q25) with TFE3 forms a ASPSCR1-TFE3 fusion protein. CC {ECO:0000269|PubMed:11244503}. CC -!- DISEASE: Note=A chromosomal aberration involving ASPSCR1 has been found CC in two patients with of papillary renal cell carcinoma. Translocation CC t(X;17)(p11.2;q25). {ECO:0000269|PubMed:11358836}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/358/ASPSCR1"; 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; AF324219; AAK08959.2; -; mRNA. DR EMBL; AK057403; BAB71472.1; -; mRNA. DR EMBL; AK057851; BAB71595.1; -; mRNA. DR EMBL; AK290624; BAF83313.1; -; mRNA. DR EMBL; BC006152; AAH06152.1; -; mRNA. DR EMBL; BC018722; AAH18722.1; -; mRNA. DR CCDS; CCDS11796.1; -. [Q9BZE9-1] DR CCDS; CCDS58611.1; -. [Q9BZE9-2] DR CCDS; CCDS82222.1; -. [Q9BZE9-3] DR RefSeq; NP_001238817.1; NM_001251888.1. [Q9BZE9-2] DR RefSeq; NP_001317457.1; NM_001330528.1. [Q9BZE9-3] DR RefSeq; NP_076988.1; NM_024083.3. [Q9BZE9-1] DR PDB; 5IFS; X-ray; 2.46 A; A/C=317-553. DR PDB; 5IFW; X-ray; 3.40 A; A=317-504. DR PDB; 7OAT; X-ray; 3.00 A; A=313-500. DR PDBsum; 5IFS; -. DR PDBsum; 5IFW; -. DR PDBsum; 7OAT; -. DR AlphaFoldDB; Q9BZE9; -. DR SMR; Q9BZE9; -. DR BioGRID; 122516; 74. DR IntAct; Q9BZE9; 37. DR MINT; Q9BZE9; -. DR STRING; 9606.ENSP00000306625; -. DR GlyCosmos; Q9BZE9; 2 sites, 1 glycan. DR GlyGen; Q9BZE9; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q9BZE9; -. DR PhosphoSitePlus; Q9BZE9; -. DR BioMuta; ASPSCR1; -. DR DMDM; 74717746; -. DR EPD; Q9BZE9; -. DR jPOST; Q9BZE9; -. DR MassIVE; Q9BZE9; -. DR MaxQB; Q9BZE9; -. DR PeptideAtlas; Q9BZE9; -. DR ProteomicsDB; 79824; -. [Q9BZE9-1] DR ProteomicsDB; 79825; -. [Q9BZE9-2] DR ProteomicsDB; 79826; -. [Q9BZE9-3] DR ProteomicsDB; 79827; -. [Q9BZE9-4] DR Pumba; Q9BZE9; -. DR Antibodypedia; 19857; 340 antibodies from 30 providers. DR DNASU; 79058; -. DR Ensembl; ENST00000306729.11; ENSP00000306625.7; ENSG00000169696.16. [Q9BZE9-2] DR Ensembl; ENST00000306739.9; ENSP00000302176.4; ENSG00000169696.16. [Q9BZE9-1] DR Ensembl; ENST00000580534.5; ENSP00000462329.1; ENSG00000169696.16. [Q9BZE9-3] DR GeneID; 79058; -. DR KEGG; hsa:79058; -. DR MANE-Select; ENST00000306739.9; ENSP00000302176.4; NM_024083.4; NP_076988.1. DR UCSC; uc002kcx.3; human. [Q9BZE9-1] DR AGR; HGNC:13825; -. DR CTD; 79058; -. DR DisGeNET; 79058; -. DR GeneCards; ASPSCR1; -. DR HGNC; HGNC:13825; ASPSCR1. DR HPA; ENSG00000169696; Low tissue specificity. DR MalaCards; ASPSCR1; -. DR MIM; 606236; gene. DR neXtProt; NX_Q9BZE9; -. DR OpenTargets; ENSG00000169696; -. DR Orphanet; 163699; Alveolar soft tissue sarcoma. DR Orphanet; 319308; MiT family translocation renal cell carcinoma. DR PharmGKB; PA25058; -. DR VEuPathDB; HostDB:ENSG00000169696; -. DR eggNOG; KOG2699; Eukaryota. DR GeneTree; ENSGT00940000156853; -. DR HOGENOM; CLU_025227_0_0_1; -. DR InParanoid; Q9BZE9; -. DR OMA; MALNVEF; -. DR OrthoDB; 103491at2759; -. DR PhylomeDB; Q9BZE9; -. DR TreeFam; TF320363; -. DR PathwayCommons; Q9BZE9; -. DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane. DR SignaLink; Q9BZE9; -. DR SIGNOR; Q9BZE9; -. DR BioGRID-ORCS; 79058; 24 hits in 1154 CRISPR screens. DR ChiTaRS; ASPSCR1; human. DR GeneWiki; ASPSCR1; -. DR GenomeRNAi; 79058; -. DR Pharos; Q9BZE9; Tbio. DR PRO; PR:Q9BZE9; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q9BZE9; Protein. DR Bgee; ENSG00000169696; Expressed in right lobe of liver and 143 other cell types or tissues. DR ExpressionAtlas; Q9BZE9; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell. DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0012506; C:vesicle membrane; IBA:GO_Central. DR GO; GO:0042593; P:glucose homeostasis; IBA:GO_Central. DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central. DR GO; GO:0031401; P:positive regulation of protein modification process; IMP:UniProtKB. DR GO; GO:0046324; P:regulation of glucose import; IEA:Ensembl. DR CDD; cd16105; Ubl_ASPSCR1_like; 1. DR CDD; cd17075; UBX1_UBXN9; 1. DR CDD; cd16118; UBX2_UBXN9; 1. DR InterPro; IPR021569; TUG-UBL1. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR InterPro; IPR001012; UBX_dom. DR PANTHER; PTHR46467; TETHER CONTAINING UBX DOMAIN FOR GLUT4; 1. DR PANTHER; PTHR46467:SF1; TETHER CONTAINING UBX DOMAIN FOR GLUT4; 1. DR Pfam; PF11470; TUG-UBL1; 1. DR Pfam; PF00789; UBX; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 2. DR PROSITE; PS50033; UBX; 1. DR Genevisible; Q9BZE9; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Chromosomal rearrangement; KW Cytoplasm; Membrane; Nucleus; Phosphoprotein; Proto-oncogene; KW Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..553 FT /note="Tether containing UBX domain for GLUT4" FT /id="PRO_0000249885" FT DOMAIN 386..462 FT /note="UBX" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215" FT REGION 182..324 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 317..380 FT /note="Interaction with GLUT4" FT /evidence="ECO:0000250" FT REGION 499..536 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 209..224 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 259..286 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 287..324 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 311..312 FT /note="Breakpoint for translocation to form ASPSCR1-TFE3" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT MOD_RES 184 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8VBT9" FT MOD_RES 275 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 500 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 502 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..77 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_020574" FT VAR_SEQ 390..425 FT /note="KVALRVLFPDRYVLQGFFRPSETVGDLRDFVRSHLG -> RRSLSLSPRLES FT VVPSQLTASSASRVQVVLLPQPPK (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_020575" FT VAR_SEQ 426..553 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_020576" FT VAR_SEQ 434 FT /note="F -> CLSSFGRMDGRGPRCFLTRRCLLSSV (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_020577" FT VAR_SEQ 451 FT /note="Q -> QPQLGDRVAPFTLGPSLKRCLGPEQRTRLPVVGDGGDVDSGRLLFWG FT PSRGRASPSTGQPPCHPVCRPSSPPSPRPSSGDPSRVKAGHKHVGTGR (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_020578" FT VARIANT 252 FT /note="L -> Q (in dbSNP:rs8074498)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_027503" FT VARIANT 318 FT /note="V -> M (in dbSNP:rs34085048)" FT /id="VAR_034745" FT VARIANT 487 FT /note="D -> E (in dbSNP:rs13087)" FT /id="VAR_027504" FT CONFLICT 257 FT /note="G -> E (in Ref. 2; BAB71595)" FT /evidence="ECO:0000305" FT CONFLICT 444 FT /note="D -> G (in Ref. 2; BAB71595)" FT /evidence="ECO:0000305" FT STRAND 323..325 FT /evidence="ECO:0007829|PDB:5IFS" FT HELIX 327..329 FT /evidence="ECO:0007829|PDB:5IFS" FT HELIX 342..345 FT /evidence="ECO:0007829|PDB:5IFS" FT HELIX 349..368 FT /evidence="ECO:0007829|PDB:5IFS" FT HELIX 374..387 FT /evidence="ECO:0007829|PDB:5IFS" FT STRAND 391..396 FT /evidence="ECO:0007829|PDB:5IFS" FT STRAND 402..407 FT /evidence="ECO:0007829|PDB:5IFS" FT HELIX 413..422 FT /evidence="ECO:0007829|PDB:5IFS" FT STRAND 424..426 FT /evidence="ECO:0007829|PDB:5IFS" FT STRAND 432..435 FT /evidence="ECO:0007829|PDB:5IFS" FT TURN 436..439 FT /evidence="ECO:0007829|PDB:5IFS" FT STRAND 445..448 FT /evidence="ECO:0007829|PDB:5IFW" FT TURN 449..453 FT /evidence="ECO:0007829|PDB:5IFS" FT STRAND 456..463 FT /evidence="ECO:0007829|PDB:5IFS" FT HELIX 467..469 FT /evidence="ECO:0007829|PDB:5IFW" FT HELIX 474..477 FT /evidence="ECO:0007829|PDB:5IFS" FT HELIX 483..494 FT /evidence="ECO:0007829|PDB:5IFS" SQ SEQUENCE 553 AA; 60183 MW; B013FDF9A48D2E5E CRC64; MAAPAGGGGS AVSVLAPNGR RHTVKVTPST VLLQVLEDTC RRQDFNPCEY DLKFQRSVLD LSLQWRFANL PNNAKLEMVP ASRSREGPEN MVRIALQLDD GSRLQDSFCS GQTLWELLSH FPQIRECLQH PGGATPVCVY TRDEVTGEAA LRGTTLQSLG LTGGSATIRF VMKCYDPVGK TPGSLGSSAS AGQAAASAPL PLESGELSRG DLSRPEDADT SGPCCEHTQE KQSTRAPAAA PFVPFSGGGQ RLGGPPGPTR PLTSSSAKLP KSLSSPGGPS KPKKSKSGQD PQQEQEQERE RDPQQEQERE RPVDREPVDR EPVVCHPDLE ERLQAWPAEL PDEFFELTVD DVRRRLAQLK SERKRLEEAP LVTKAFREAQ IKEKLERYPK VALRVLFPDR YVLQGFFRPS ETVGDLRDFV RSHLGNPELS FYLFITPPKT VLDDHTQTLF QANLFPAALV HLGAEEPAGV YLEPGLLEHA ISPSAADVLV ARYMSRAAGS PSPLPAPDPA PKSEPAAEEG ALVPPEPIPG TAQPVKRSLG KVPKWLKLPA SKR //