SCAF4_HUMAN
ID SCAF4_HUMAN Reviewed; 1147 AA.
AC O95104; C9JLZ0; Q0P5W8; Q6P1M5; Q8N3I8; Q9UFM1; Q9ULP8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=SR-related and CTD-associated factor 4 {ECO:0000303|PubMed:31104839};
DE AltName: Full=CTD-binding SR-like protein RA4 {ECO:0000305};
DE AltName: Full=Splicing factor, arginine/serine-rich 15 {ECO:0000305};
GN Name=SCAF4 {ECO:0000303|PubMed:31104839, ECO:0000312|HGNC:HGNC:19304};
GN Synonyms=KIAA1172 {ECO:0000303|PubMed:10574461},
GN SFRS15 {ECO:0000312|HGNC:HGNC:19304};
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).
RA Tassone F., Villard L., Gardiner K.;
RT "Sequence, genomic organization and map localization of the human SR
RT protein gene rA4.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Trachea;
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 2).
RC TISSUE=Melanoma, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Uterus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-1147 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-656, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-49, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-656, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154 AND SER-1004, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND IDENTIFICATION BY
RP 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).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH POLR2A.
RX PubMed=31104839; DOI=10.1016/j.cell.2019.04.038;
RA Gregersen L.H., Mitter R., Ugalde A.P., Nojima T., Proudfoot N.J.,
RA Agami R., Stewart A., Svejstrup J.Q.;
RT "SCAF4 and SCAF8, mRNA anti-terminator proteins.";
RL Cell 0:0-0(2019).
CC -!- FUNCTION: Anti-terminator protein required to prevent early mRNA
CC termination during transcription (PubMed:31104839). Together with
CC SCAF8, acts by suppressing the use of early, alternative poly(A) sites,
CC thereby preventing the accumulation of non-functional truncated
CC proteins (PubMed:31104839). Mechanistically, associates with the
CC phosphorylated C-terminal heptapeptide repeat domain (CTD) of the
CC largest RNA polymerase II subunit (POLR2A), and subsequently binds
CC nascent RNA upstream of early polyadenylation sites to prevent
CC premature mRNA transcript cleavage and polyadenylation
CC (PubMed:31104839). Independently of SCAF8, also acts as a suppressor of
CC transcriptional readthrough (PubMed:31104839).
CC {ECO:0000269|PubMed:31104839}.
CC -!- SUBUNIT: Interacts with POLR2A; via C-terminal heptapeptide repeat
CC domain (CTD) phosphorylated at 'Ser-2' and 'Ser-5'.
CC {ECO:0000269|PubMed:31104839}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31104839}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O95104-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95104-2; Sequence=VSP_005879;
CC Name=3;
CC IsoId=O95104-3; Sequence=VSP_047351;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD09327.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF023142; AAD09327.1; ALT_INIT; mRNA.
DR EMBL; AK308406; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL834304; CAD38974.2; -; mRNA.
DR EMBL; AL117417; CAB55911.1; ALT_SEQ; mRNA.
DR EMBL; AP001711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014921; AAH14921.1; -; mRNA.
DR EMBL; BC052286; AAH52286.1; -; mRNA.
DR EMBL; BC064990; AAH64990.1; -; mRNA.
DR EMBL; AB032998; BAA86486.1; -; mRNA.
DR CCDS; CCDS33537.1; -. [O95104-1]
DR CCDS; CCDS46644.1; -. [O95104-2]
DR CCDS; CCDS54482.1; -. [O95104-3]
DR RefSeq; NP_001138916.1; NM_001145444.1. [O95104-3]
DR RefSeq; NP_001138917.1; NM_001145445.1. [O95104-2]
DR RefSeq; NP_065757.1; NM_020706.2. [O95104-1]
DR PDB; 6XKB; X-ray; 1.60 A; A/B/C/D/E=1-139.
DR PDBsum; 6XKB; -.
DR AlphaFoldDB; O95104; -.
DR SMR; O95104; -.
DR BioGRID; 121536; 109.
DR IntAct; O95104; 21.
DR MINT; O95104; -.
DR STRING; 9606.ENSP00000286835; -.
DR GlyGen; O95104; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95104; -.
DR PhosphoSitePlus; O95104; -.
DR BioMuta; SCAF4; -.
DR EPD; O95104; -.
DR jPOST; O95104; -.
DR MassIVE; O95104; -.
DR MaxQB; O95104; -.
DR PaxDb; O95104; -.
DR PeptideAtlas; O95104; -.
DR PRIDE; O95104; -.
DR ProteomicsDB; 10774; -.
DR ProteomicsDB; 50653; -. [O95104-1]
DR ProteomicsDB; 50654; -. [O95104-2]
DR Antibodypedia; 6761; 103 antibodies from 24 providers.
DR DNASU; 57466; -.
DR Ensembl; ENST00000286835.12; ENSP00000286835.7; ENSG00000156304.15. [O95104-1]
DR Ensembl; ENST00000399804.5; ENSP00000382703.1; ENSG00000156304.15. [O95104-2]
DR Ensembl; ENST00000434667.3; ENSP00000402377.2; ENSG00000156304.15. [O95104-3]
DR GeneID; 57466; -.
DR KEGG; hsa:57466; -.
DR MANE-Select; ENST00000286835.12; ENSP00000286835.7; NM_020706.2; NP_065757.1.
DR UCSC; uc002ypd.3; human. [O95104-1]
DR CTD; 57466; -.
DR DisGeNET; 57466; -.
DR GeneCards; SCAF4; -.
DR HGNC; HGNC:19304; SCAF4.
DR HPA; ENSG00000156304; Low tissue specificity.
DR MIM; 616023; gene.
DR neXtProt; NX_O95104; -.
DR OpenTargets; ENSG00000156304; -.
DR PharmGKB; PA134903281; -.
DR VEuPathDB; HostDB:ENSG00000156304; -.
DR eggNOG; KOG0132; Eukaryota.
DR GeneTree; ENSGT00530000063946; -.
DR HOGENOM; CLU_005263_0_1_1; -.
DR InParanoid; O95104; -.
DR OMA; AEGDKNH; -.
DR OrthoDB; 821342at2759; -.
DR PhylomeDB; O95104; -.
DR TreeFam; TF324527; -.
DR PathwayCommons; O95104; -.
DR SignaLink; O95104; -.
DR BioGRID-ORCS; 57466; 105 hits in 1084 CRISPR screens.
DR ChiTaRS; SCAF4; human.
DR GenomeRNAi; 57466; -.
DR Pharos; O95104; Tbio.
DR PRO; PR:O95104; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; O95104; protein.
DR Bgee; ENSG00000156304; Expressed in tendon of biceps brachii and 179 other tissues.
DR Genevisible; O95104; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:1990269; F:RNA polymerase II C-terminal domain phosphoserine binding; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:Ensembl.
DR GO; GO:2000805; P:negative regulation of termination of RNA polymerase II transcription, poly(A)-coupled; IDA:UniProtKB.
DR CDD; cd12461; RRM_SCAF4; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034369; SCAF4_RRM.
DR Pfam; PF04818; CID; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00582; RPR; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51391; CID; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..1147
FT /note="SR-related and CTD-associated factor 4"
FT /id="PRO_0000081943"
FT DOMAIN 1..139
FT /note="CID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT DOMAIN 508..582
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 145..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..477
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..917
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..976
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1087
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1004
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 38..52
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047351"
FT VAR_SEQ 766..788
FT /note="STIAGINEDTTKDLSIGNPIPTV -> L (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10574461,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_005879"
FT VARIANT 846
FT /note="S -> Y (in dbSNP:rs12152067)"
FT /id="VAR_052234"
FT CONFLICT 1
FT /note="M -> W (in Ref. 1; AAD09327)"
FT /evidence="ECO:0000305"
FT CONFLICT 260..264
FT /note="Missing (in Ref. 3; CAB55911)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="T -> I (in Ref. 1; AAD09327)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="T -> A (in Ref. 1; AAD09327)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="T -> A (in Ref. 1; AAD09327)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="V -> L (in Ref. 6; BAA86486)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="H -> Y (in Ref. 1; AAD09327)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="L -> V (in Ref. 1; AAD09327)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="N -> T (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 598..600
FT /note="GVT -> CVI (in Ref. 1; AAD09327)"
FT /evidence="ECO:0000305"
FT CONFLICT 604..606
FT /note="WDK -> CDN (in Ref. 1; AAD09327)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="L -> M (in Ref. 1; AAD09327)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="C -> Y (in Ref. 1; AAD09327)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="D -> N (in Ref. 3; AK308406)"
FT /evidence="ECO:0000305"
FT CONFLICT 808..826
FT /note="AVPPAAPTNLPTPPVTQPV -> TCCTHESAHPSCNPACLPC (in Ref.
FT 1; AAD09327)"
FT /evidence="ECO:0000305"
FT CONFLICT 844
FT /note="A -> E (in Ref. 1; AAD09327)"
FT /evidence="ECO:0000305"
FT CONFLICT 1139
FT /note="S -> G (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 1..12
FT /evidence="ECO:0007829|PDB:6XKB"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:6XKB"
FT HELIX 23..35
FT /evidence="ECO:0007829|PDB:6XKB"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:6XKB"
FT HELIX 40..53
FT /evidence="ECO:0007829|PDB:6XKB"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:6XKB"
FT HELIX 59..77
FT /evidence="ECO:0007829|PDB:6XKB"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:6XKB"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:6XKB"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:6XKB"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:6XKB"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:6XKB"
FT HELIX 125..134
FT /evidence="ECO:0007829|PDB:6XKB"
SQ SEQUENCE 1147 AA; 125869 MW; DED5EEAB45DB4B83 CRC64;
MDAVNAFNQE LFSLMDMKPP ISRAKMILIT KAAIKAIKLY KHVVQIVEKF IKKCKPEYKV
PGLYVIDSIV RQSRHQFGTD KDVFGPRFSK NITATFQYLY LCPSEDKSKI VRVLNLWQKN
GVFKIEIIQP LLDMAAGTSN AAPVAENVTN NEGSPPPPVK VSSEPPTQAT PNSVPAVPQL
PSSDAFAAVA QLFQTTQGQQ LQQILQTFQQ PPKPQSPALD NAVMAQVQAI TAQLKTTPTQ
PSEQKAAFPP PEQKTAFDKK LLDRFDYDDE PEAVEESKKE DTTAVTTTAP AAAVPPAPTA
TVPAAAAPAA ASPPPPQAPF GFPGDGMQQP AYTQHQNMDQ FQPRMMGIQQ DPMHHQVPLP
PNGQMPGFGL LPTPPFPPMA QPVIPPTPPV QQPFQASFQA QNEPLTQKPH QQEMEVEQPC
IQEVKRHMSD NRKSRSRSAS RSPKRRRSRS GSRSRRSRHR RSRSRSRDRR RHSPRSRSQE
RRDREKERER RQKGLPQVKP ETASVCSTTL WVGQLDKRTT QQDVASLLEE FGPIESINMI
PPRGCAYIVM VHRQDAYRAL QKLSRGNYKV NQKSIKIAWA LNKGIKADYK QYWDVELGVT
YIPWDKVKPE ELESFCEGGM LDSDTLNPDW KGIPKKPENE VAQNGGAETS HTEPVSPIPK
PLPVPVPPIP VPAPITVPPP QVPPHQPGPP VVGALQPPAF TPPLGIPPPG FGPGVPPPPP
PPPFLRPGFN PMHLPPGFLP PGPPPPITPP VSIPPPHTPP ISIPNSTIAG INEDTTKDLS
IGNPIPTVVS GARGNAESGD SVKMYGSAVP PAAPTNLPTP PVTQPVSLLG TQGVAPGPVI
GLQAPSTGLL GARPGLIPLQ RPPGMPPPHL QRFPLMPPRP MPPHMMHRGP PPGPGGFAMP
PPHGMKGPFP PHGPFVRPGG MPGLGGPGPG PGGPEDRDGR QQPPQQPQQQ PQPQAPQQPQ
QQQQQQPPPS QQPPPTQQQP QQFRNDNRQQ FNSGRDQERF GRRSFGNRVE NDRERYGNRN
DDRDNSNRDR REWGRRSPDR DRHRDLEERN RRSSGHRDRE RDSRDRESRR EKEEARGKEK
PEVTDRAGGN KTVEPPISQV GNVDTASELE KGVSEAAVLK PSEELPAEAT SSVEPEKDSG
SAAEAPR
