PTBP2_HUMAN
ID PTBP2_HUMAN Reviewed; 531 AA.
AC Q9UKA9; Q8N0Z1; Q8N160; Q8NFB0; Q8NFB1; Q969N9; Q96Q76;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Polypyrimidine tract-binding protein 2 {ECO:0000305};
DE AltName: Full=Neural polypyrimidine tract-binding protein;
DE AltName: Full=Neurally-enriched homolog of PTB;
DE AltName: Full=PTB-like protein;
GN Name=PTBP2 {ECO:0000312|HGNC:HGNC:17662}; Synonyms=NPTB, PTB, PTBLP;
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), PROTEIN SEQUENCE OF 55-65; 210-215;
RP 216-235; 370-374; 404-411; 431-440 AND 487-492, FUNCTION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH HNRPH1 AND KHSRP.
RC TISSUE=Retinoblastoma;
RX PubMed=11003644; DOI=10.1128/mcb.20.20.7463-7479.2000;
RA Markovtsov V., Nikolic J.M., Goldman J.A., Turck C.W., Chou M.-Y.,
RA Black D.L.;
RT "Cooperative assembly of an hnRNP complex induced by a tissue-specific
RT homolog of polypyrimidine tract binding protein.";
RL Mol. Cell. Biol. 20:7463-7479(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), AND ALTERNATIVE SPLICING
RP (ISOFORMS 3 AND 6).
RC TISSUE=Retina;
RX PubMed=11694331; DOI=10.1016/s0165-5728(01)00427-1;
RA Tateiwa H., Gotoh N., Ichikawa M., Kikuchi T., Yoshimura N.;
RT "Molecular cloning and characterization of human PTB-like protein: a
RT possible retinal autoantigen of cancer-associated retinopathy.";
RL J. Neuroimmunol. 120:161-169(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 282-531 (ISOFORMS 5 AND 6), ALTERNATIVE SPLICING (ISOFORM 2), AND
RP TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma, Lung, and Retinoblastoma;
RX PubMed=12213192; DOI=10.1006/geno.2002.6826;
RA Rahman L., Bliskovski V., Reinhold W., Zajac-Kaye M.;
RT "Alternative splicing of brain-specific PTB defines a tissue-specific
RT isoform pattern that predicts distinct functional roles.";
RL Genomics 80:245-249(2002).
RN [4]
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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [6]
RP FUNCTION.
RX PubMed=12667457; DOI=10.1016/s1097-2765(03)00093-5;
RA Mitchell S.A., Spriggs K.A., Coldwell M.J., Jackson R.J., Willis A.E.;
RT "The Apaf-1 internal ribosome entry segment attains the correct structural
RT conformation for function via interactions with PTB and unr.";
RL Mol. Cell 11:757-771(2003).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [8]
RP IDENTIFICATION IN A MRNP COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19029303; DOI=10.1261/rna.1175909;
RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A.,
RA Buchmeier S., Wahle E., Huettelmaiery S.;
RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs.";
RL RNA 15:104-115(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [12]
RP STRUCTURE BY NMR OF 51-138.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA-binding domain in PTB-like protein.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: RNA-binding protein which binds to intronic polypyrimidine
CC tracts and mediates negative regulation of exons splicing. May
CC antagonize in a tissue-specific manner the ability of NOVA1 to activate
CC exon selection. In addition to its function in pre-mRNA splicing, plays
CC also a role in the regulation of translation.
CC {ECO:0000250|UniProtKB:Q91Z31, ECO:0000269|PubMed:11003644,
CC ECO:0000269|PubMed:12667457}.
CC -!- FUNCTION: [Isoform 5]: Reduced affinity for RNA.
CC {ECO:0000269|PubMed:12213192}.
CC -!- SUBUNIT: Monomer. Interacts with NOVA1; the interaction is direct.
CC Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1,
CC HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and
CC YBX1. Part of a ternary complex containing KHSRP and HNRPH1
CC (PubMed:11003644, PubMed:19029303). Interacts with NOVA2; the
CC interaction is direct (By similarity). {ECO:0000250|UniProtKB:Q91Z31,
CC ECO:0000269|PubMed:11003644, ECO:0000269|PubMed:19029303}.
CC -!- INTERACTION:
CC Q9UKA9-2; P35637: FUS; NbExp=3; IntAct=EBI-12255608, EBI-400434;
CC Q9UKA9-2; P43243: MATR3; NbExp=3; IntAct=EBI-12255608, EBI-352602;
CC Q9UKA9-2; P98175: RBM10; NbExp=3; IntAct=EBI-12255608, EBI-721525;
CC Q9UKA9-2; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-12255608, EBI-11987469;
CC Q9UKA9-2; P09012: SNRPA; NbExp=3; IntAct=EBI-12255608, EBI-607085;
CC Q9UKA9-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-12255608, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91Z31}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=nPTB1;
CC IsoId=Q9UKA9-1; Sequence=Displayed;
CC Name=2; Synonyms=nPTB2, PTBPLP-L;
CC IsoId=Q9UKA9-2; Sequence=VSP_018018;
CC Name=3; Synonyms=nPTB3, PTBPLP-L';
CC IsoId=Q9UKA9-3; Sequence=VSP_018015, VSP_018018;
CC Name=4; Synonyms=nPTB4;
CC IsoId=Q9UKA9-4; Sequence=VSP_018015;
CC Name=5; Synonyms=nPTB5, nPTB7, PTBPLP-S;
CC IsoId=Q9UKA9-5; Sequence=VSP_018016, VSP_018017;
CC Name=6; Synonyms=nPTB6, nPTB8, PTBPLP-S';
CC IsoId=Q9UKA9-6; Sequence=VSP_018015, VSP_018016, VSP_018017;
CC -!- TISSUE SPECIFICITY: Mainly expressed in brain although also detected in
CC other tissues like heart and skeletal muscle. Isoform 1 and isoform 2
CC are specifically expressed in neuronal tissues. Isoform 3 and isoform 4
CC are expressed in non-neuronal tissues. Isoform 5 and isoform 6 are
CC truncated forms expressed in non-neuronal tissues.
CC {ECO:0000269|PubMed:11003644, ECO:0000269|PubMed:12213192}.
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DR EMBL; AF176085; AAF14284.1; -; mRNA.
DR EMBL; AB051232; BAB71742.1; -; mRNA.
DR EMBL; AB051233; BAB71743.1; -; mRNA.
DR EMBL; AF530580; AAM94624.1; -; mRNA.
DR EMBL; AF530581; AAM94625.1; -; mRNA.
DR EMBL; AF530582; AAM94626.1; -; mRNA.
DR EMBL; AF530583; AAM94627.1; -; mRNA.
DR EMBL; BK000526; DAA00060.1; -; mRNA.
DR EMBL; AL357150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016582; AAH16582.1; -; mRNA.
DR CCDS; CCDS72828.1; -. [Q9UKA9-3]
DR CCDS; CCDS72829.1; -. [Q9UKA9-4]
DR CCDS; CCDS72830.1; -. [Q9UKA9-2]
DR CCDS; CCDS754.1; -. [Q9UKA9-1]
DR RefSeq; NP_001287914.1; NM_001300985.1. [Q9UKA9-3]
DR RefSeq; NP_001287915.1; NM_001300986.1.
DR RefSeq; NP_001287916.1; NM_001300987.1.
DR RefSeq; NP_001287917.1; NM_001300988.1. [Q9UKA9-4]
DR RefSeq; NP_001287918.1; NM_001300989.1. [Q9UKA9-2]
DR RefSeq; NP_001287919.1; NM_001300990.1.
DR RefSeq; NP_067013.1; NM_021190.3. [Q9UKA9-1]
DR PDB; 2CQ1; NMR; -; A=51-138.
DR PDB; 2MJU; NMR; -; A=325-531.
DR PDB; 4CQ1; X-ray; 1.69 A; A/B/C/D/E/F/G/H=336-531.
DR PDBsum; 2CQ1; -.
DR PDBsum; 2MJU; -.
DR PDBsum; 4CQ1; -.
DR AlphaFoldDB; Q9UKA9; -.
DR BMRB; Q9UKA9; -.
DR SASBDB; Q9UKA9; -.
DR SMR; Q9UKA9; -.
DR BioGRID; 121796; 46.
DR CORUM; Q9UKA9; -.
DR IntAct; Q9UKA9; 33.
DR MINT; Q9UKA9; -.
DR STRING; 9606.ENSP00000359216; -.
DR GlyConnect; 2061; 1 N-Linked glycan (1 site).
DR GlyGen; Q9UKA9; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q9UKA9; -.
DR MetOSite; Q9UKA9; -.
DR PhosphoSitePlus; Q9UKA9; -.
DR SwissPalm; Q9UKA9; -.
DR BioMuta; PTBP2; -.
DR DMDM; 74761983; -.
DR REPRODUCTION-2DPAGE; IPI00647067; -.
DR EPD; Q9UKA9; -.
DR jPOST; Q9UKA9; -.
DR MassIVE; Q9UKA9; -.
DR MaxQB; Q9UKA9; -.
DR PaxDb; Q9UKA9; -.
DR PeptideAtlas; Q9UKA9; -.
DR PRIDE; Q9UKA9; -.
DR ProteomicsDB; 84754; -. [Q9UKA9-1]
DR ProteomicsDB; 84755; -. [Q9UKA9-2]
DR ProteomicsDB; 84756; -. [Q9UKA9-3]
DR ProteomicsDB; 84757; -. [Q9UKA9-4]
DR ProteomicsDB; 84758; -. [Q9UKA9-5]
DR ProteomicsDB; 84759; -. [Q9UKA9-6]
DR Antibodypedia; 19957; 230 antibodies from 31 providers.
DR DNASU; 58155; -.
DR Ensembl; ENST00000370197.5; ENSP00000359216.1; ENSG00000117569.19. [Q9UKA9-3]
DR Ensembl; ENST00000370198.5; ENSP00000359217.1; ENSG00000117569.19. [Q9UKA9-4]
DR Ensembl; ENST00000476419.5; ENSP00000501834.1; ENSG00000117569.19. [Q9UKA9-5]
DR Ensembl; ENST00000609116.5; ENSP00000477024.1; ENSG00000117569.19. [Q9UKA9-2]
DR Ensembl; ENST00000674951.1; ENSP00000502818.1; ENSG00000117569.19. [Q9UKA9-1]
DR GeneID; 58155; -.
DR KEGG; hsa:58155; -.
DR MANE-Select; ENST00000674951.1; ENSP00000502818.1; NM_021190.4; NP_067013.1.
DR UCSC; uc001drn.3; human. [Q9UKA9-1]
DR CTD; 58155; -.
DR DisGeNET; 58155; -.
DR GeneCards; PTBP2; -.
DR HGNC; HGNC:17662; PTBP2.
DR HPA; ENSG00000117569; Low tissue specificity.
DR MIM; 608449; gene.
DR neXtProt; NX_Q9UKA9; -.
DR OpenTargets; ENSG00000117569; -.
DR PharmGKB; PA33935; -.
DR VEuPathDB; HostDB:ENSG00000117569; -.
DR eggNOG; KOG1190; Eukaryota.
DR GeneTree; ENSGT01050000244924; -.
DR HOGENOM; CLU_015171_7_0_1; -.
DR InParanoid; Q9UKA9; -.
DR OMA; NLGESHH; -.
DR PhylomeDB; Q9UKA9; -.
DR TreeFam; TF319824; -.
DR PathwayCommons; Q9UKA9; -.
DR SignaLink; Q9UKA9; -.
DR SIGNOR; Q9UKA9; -.
DR BioGRID-ORCS; 58155; 18 hits in 1087 CRISPR screens.
DR ChiTaRS; PTBP2; human.
DR EvolutionaryTrace; Q9UKA9; -.
DR GeneWiki; PTBP2; -.
DR GenomeRNAi; 58155; -.
DR Pharos; Q9UKA9; Tbio.
DR PRO; PR:Q9UKA9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UKA9; protein.
DR Bgee; ENSG00000117569; Expressed in cortical plate and 195 other tissues.
DR ExpressionAtlas; Q9UKA9; baseline and differential.
DR Genevisible; Q9UKA9; HS.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR GO; GO:0006376; P:mRNA splice site selection; IEA:Ensembl.
DR GO; GO:0033119; P:negative regulation of RNA splicing; IDA:UniProtKB.
DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; IEA:Ensembl.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR CDD; cd12778; RRM1_PTBP2; 1.
DR CDD; cd12693; RRM2_PTBP1_like; 1.
DR CDD; cd12696; RRM3_PTBP2; 1.
DR CDD; cd12702; RRM4_PTBP2; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR006536; HnRNP-L/PTB.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR021790; PTBP1-like_RRM2.
DR InterPro; IPR034798; PTBP1/2/3_RRM2.
DR InterPro; IPR035002; PTBP2_RRM1.
DR InterPro; IPR034799; PTBP2_RRM3.
DR InterPro; IPR034800; PTBP2_RRM4.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF11835; RRM_8; 1.
DR SMART; SM00360; RRM; 4.
DR SUPFAM; SSF54928; SSF54928; 4.
DR TIGRFAMs; TIGR01649; hnRNP-L_PTB; 1.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..531
FT /note="Polypyrimidine tract-binding protein 2"
FT /id="PRO_0000232928"
FT DOMAIN 59..133
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 181..257
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 338..412
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 455..529
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91Z31"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91Z31"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 302
FT /note="A -> GLPVAA (in isoform 3, isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12213192"
FT /id="VSP_018015"
FT VAR_SEQ 349..356
FT /note="MVTPQSLF -> VFMEMCSV (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:11694331,
FT ECO:0000303|PubMed:12213192"
FT /id="VSP_018016"
FT VAR_SEQ 357..531
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:11694331,
FT ECO:0000303|PubMed:12213192"
FT /id="VSP_018017"
FT VAR_SEQ 489
FT /note="Q -> QR (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11694331,
FT ECO:0000303|PubMed:12213192, ECO:0000303|PubMed:15489334"
FT /id="VSP_018018"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:2CQ1"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:2CQ1"
FT TURN 78..82
FT /evidence="ECO:0007829|PDB:2CQ1"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:2CQ1"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:2CQ1"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:2CQ1"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:2CQ1"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:2CQ1"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:4CQ1"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:4CQ1"
FT HELIX 352..359
FT /evidence="ECO:0007829|PDB:4CQ1"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:4CQ1"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:4CQ1"
FT STRAND 374..384
FT /evidence="ECO:0007829|PDB:4CQ1"
FT HELIX 385..395
FT /evidence="ECO:0007829|PDB:4CQ1"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:2MJU"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:4CQ1"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:2MJU"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:2MJU"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:4CQ1"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:2MJU"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:4CQ1"
FT STRAND 447..450
FT /evidence="ECO:0007829|PDB:2MJU"
FT STRAND 455..460
FT /evidence="ECO:0007829|PDB:4CQ1"
FT HELIX 468..476
FT /evidence="ECO:0007829|PDB:4CQ1"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:4CQ1"
FT STRAND 482..487
FT /evidence="ECO:0007829|PDB:4CQ1"
FT STRAND 494..500
FT /evidence="ECO:0007829|PDB:4CQ1"
FT HELIX 501..511
FT /evidence="ECO:0007829|PDB:4CQ1"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:4CQ1"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:4CQ1"
SQ SEQUENCE 531 AA; 57491 MW; 57ADA23F422AE02A CRC64;
MDGIVTEVAV GVKRGSDELL SGSVLSSPNS NMSSMVVTAN GNDSKKFKGE DKMDGAPSRV
LHIRKLPGEV TETEVIALGL PFGKVTNILM LKGKNQAFLE LATEEAAITM VNYYSAVTPH
LRNQPIYIQY SNHKELKTDN TLNQRAQAVL QAVTAVQTAN TPLSGTTVSE SAVTPAQSPV
LRIIIDNMYY PVTLDVLHQI FSKFGAVLKI ITFTKNNQFQ ALLQYGDPVN AQQAKLALDG
QNIYNACCTL RIDFSKLVNL NVKYNNDKSR DYTRPDLPSG DGQPALDPAI AAAFAKETSL
LAVPGALSPL AIPNAAAAAA AAAAGRVGMP GVSAGGNTVL LVSNLNEEMV TPQSLFTLFG
VYGDVQRVKI LYNKKDSALI QMADGNQSQL AMNHLNGQKM YGKIIRVTLS KHQTVQLPRE
GLDDQGLTKD FGNSPLHRFK KPGSKNFQNI FPPSATLHLS NIPPSVAEED LRTLFANTGG
TVKAFKFFQD HKMALLQMAT VEEAIQALID LHNYNLGENH HLRVSFSKST I
