INT7_HUMAN
ID INT7_HUMAN Reviewed; 962 AA.
AC Q9NVH2; B4DLZ6; B7WNP6; B7WPB6; Q8N4K7; Q8WUH5; Q9H9V3; Q9NVU5; Q9UFC6;
AC Q9UFM3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Integrator complex subunit 7;
DE Short=Int7;
GN Name=INTS7; Synonyms=C1orf73;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ARG-425.
RC TISSUE=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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ARG-425.
RC TISSUE=Skin, 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 204-962 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE INTEGRATOR
RP COMPLEX.
RX PubMed=16239144; DOI=10.1016/j.cell.2005.08.019;
RA Baillat D., Hakimi M.-A., Naeaer A.M., Shilatifard A., Cooch N.,
RA Shiekhattar R.;
RT "Integrator, a multiprotein mediator of small nuclear RNA processing,
RT associates with the C-terminal repeat of RNA polymerase II.";
RL Cell 123:265-276(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
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 [10]
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 [11]
RP FUNCTION, INTERACTION WITH NABP2, AND SUBCELLULAR LOCATION.
RX PubMed=21659603; DOI=10.1126/science.1203430;
RA Cotta-Ramusino C., McDonald E.R. III, Hurov K., Sowa M.E., Harper J.W.,
RA Elledge S.J.;
RT "A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1
RT interacting protein required for ATR signaling.";
RL Science 332:1313-1317(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338 AND SER-809, 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 [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23904267; DOI=10.1091/mbc.e13-05-0254;
RA Jodoin J.N., Sitaram P., Albrecht T.R., May S.B., Shboul M., Lee E.,
RA Reversade B., Wagner E.J., Lee L.A.;
RT "Nuclear-localized Asunder regulates cytoplasmic dynein localization via
RT its role in the integrator complex.";
RL Mol. Biol. Cell 24:2954-2965(2013).
CC -!- FUNCTION: Component of the Integrator (INT) complex, a complex involved
CC in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their
CC 3'-box-dependent processing. The Integrator complex is associated with
CC the C-terminal domain (CTD) of RNA polymerase II largest subunit
CC (POLR2A) and is recruited to the U1 and U2 snRNAs genes (Probable).
CC Plays a role in DNA damage response (DDR) signaling during the S phase
CC (PubMed:21659603). May be not involved in the recruitment of
CC cytoplasmic dynein to the nuclear envelope by different components of
CC the INT complex (PubMed:23904267). {ECO:0000269|PubMed:21659603,
CC ECO:0000269|PubMed:23904267, ECO:0000305|PubMed:16239144}.
CC -!- SUBUNIT: Belongs to the multiprotein complex Integrator, at least
CC composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8,
CC INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12. Interacts with NABP2.
CC {ECO:0000269|PubMed:16239144, ECO:0000269|PubMed:21659603}.
CC -!- INTERACTION:
CC Q9NVH2; P35219: CA8; NbExp=3; IntAct=EBI-11276282, EBI-718700;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21659603}. Chromosome
CC {ECO:0000269|PubMed:21659603}. Cytoplasm {ECO:0000269|PubMed:23904267}.
CC Note=Localizes to sites of DNA damage in a H2AX-independent manner.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NVH2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NVH2-2; Sequence=VSP_021463;
CC Name=3;
CC IsoId=Q9NVH2-3; Sequence=VSP_021464;
CC Name=4;
CC IsoId=Q9NVH2-4; Sequence=VSP_043201;
CC -!- SIMILARITY: Belongs to the Integrator subunit 7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91650.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14116.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AK001363; BAA91650.1; ALT_SEQ; mRNA.
DR EMBL; AK001598; BAA91779.1; -; mRNA.
DR EMBL; AK022509; BAB14067.1; -; mRNA.
DR EMBL; AK022589; BAB14116.1; ALT_INIT; mRNA.
DR EMBL; AK297225; BAG59708.1; -; mRNA.
DR EMBL; AL117576; CAB56000.1; -; mRNA.
DR EMBL; AM392654; CAL37532.1; -; mRNA.
DR EMBL; AC092814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471100; EAW93406.1; -; Genomic_DNA.
DR EMBL; BC020523; AAH20523.1; -; mRNA.
DR EMBL; BC030716; AAH30716.1; -; mRNA.
DR EMBL; BC033918; AAH33918.1; -; mRNA.
DR EMBL; AL133049; CAB61376.1; -; mRNA.
DR EMBL; BK005725; DAA05725.1; -; mRNA.
DR CCDS; CCDS1501.1; -. [Q9NVH2-1]
DR CCDS; CCDS55683.1; -. [Q9NVH2-4]
DR CCDS; CCDS55684.1; -. [Q9NVH2-3]
DR CCDS; CCDS55685.1; -. [Q9NVH2-2]
DR PIR; T17310; T17310.
DR PIR; T42652; T42652.
DR RefSeq; NP_001186738.1; NM_001199809.1. [Q9NVH2-4]
DR RefSeq; NP_001186740.1; NM_001199811.1. [Q9NVH2-2]
DR RefSeq; NP_001186741.1; NM_001199812.1. [Q9NVH2-3]
DR RefSeq; NP_056249.1; NM_015434.3. [Q9NVH2-1]
DR PDB; 7CUN; EM; 3.50 A; G=1-962.
DR PDB; 7PKS; EM; 3.60 A; g=1-962.
DR PDBsum; 7CUN; -.
DR PDBsum; 7PKS; -.
DR AlphaFoldDB; Q9NVH2; -.
DR SMR; Q9NVH2; -.
DR BioGRID; 117404; 106.
DR ComplexPortal; CPX-6441; Integrator complex.
DR CORUM; Q9NVH2; -.
DR IntAct; Q9NVH2; 50.
DR MINT; Q9NVH2; -.
DR STRING; 9606.ENSP00000355961; -.
DR iPTMnet; Q9NVH2; -.
DR PhosphoSitePlus; Q9NVH2; -.
DR BioMuta; INTS7; -.
DR DMDM; 74752993; -.
DR EPD; Q9NVH2; -.
DR jPOST; Q9NVH2; -.
DR MassIVE; Q9NVH2; -.
DR MaxQB; Q9NVH2; -.
DR PaxDb; Q9NVH2; -.
DR PeptideAtlas; Q9NVH2; -.
DR PRIDE; Q9NVH2; -.
DR ProteomicsDB; 82799; -. [Q9NVH2-1]
DR ProteomicsDB; 82800; -. [Q9NVH2-2]
DR ProteomicsDB; 82801; -. [Q9NVH2-3]
DR ProteomicsDB; 82802; -. [Q9NVH2-4]
DR Antibodypedia; 34604; 60 antibodies from 19 providers.
DR DNASU; 25896; -.
DR Ensembl; ENST00000366992.7; ENSP00000355959.3; ENSG00000143493.13. [Q9NVH2-3]
DR Ensembl; ENST00000366993.7; ENSP00000355960.3; ENSG00000143493.13. [Q9NVH2-2]
DR Ensembl; ENST00000366994.8; ENSP00000355961.3; ENSG00000143493.13. [Q9NVH2-1]
DR Ensembl; ENST00000440600.6; ENSP00000388908.2; ENSG00000143493.13. [Q9NVH2-4]
DR GeneID; 25896; -.
DR KEGG; hsa:25896; -.
DR MANE-Select; ENST00000366994.8; ENSP00000355961.3; NM_015434.4; NP_056249.1.
DR UCSC; uc001hiw.3; human. [Q9NVH2-1]
DR CTD; 25896; -.
DR DisGeNET; 25896; -.
DR GeneCards; INTS7; -.
DR HGNC; HGNC:24484; INTS7.
DR HPA; ENSG00000143493; Low tissue specificity.
DR MIM; 611350; gene.
DR neXtProt; NX_Q9NVH2; -.
DR OpenTargets; ENSG00000143493; -.
DR PharmGKB; PA142672522; -.
DR VEuPathDB; HostDB:ENSG00000143493; -.
DR eggNOG; KOG1988; Eukaryota.
DR GeneTree; ENSGT00390000011724; -.
DR HOGENOM; CLU_013157_0_0_1; -.
DR InParanoid; Q9NVH2; -.
DR OMA; FAHIIES; -.
DR OrthoDB; 1131967at2759; -.
DR PhylomeDB; Q9NVH2; -.
DR TreeFam; TF106105; -.
DR PathwayCommons; Q9NVH2; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR SignaLink; Q9NVH2; -.
DR SIGNOR; Q9NVH2; -.
DR BioGRID-ORCS; 25896; 660 hits in 1080 CRISPR screens.
DR ChiTaRS; INTS7; human.
DR GeneWiki; INTS7; -.
DR GenomeRNAi; 25896; -.
DR Pharos; Q9NVH2; Tdark.
DR PRO; PR:Q9NVH2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NVH2; protein.
DR Bgee; ENSG00000143493; Expressed in ganglionic eminence and 163 other tissues.
DR ExpressionAtlas; Q9NVH2; baseline and differential.
DR Genevisible; Q9NVH2; HS.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0032039; C:integrator complex; IDA:HGNC-UCL.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IDA:UniProtKB.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0034472; P:snRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0016180; P:snRNA processing; IDA:HGNC-UCL.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033060; INTS7.
DR PANTHER; PTHR13322; PTHR13322; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; Cytoplasm; DNA damage;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..962
FT /note="Integrator complex subunit 7"
FT /id="PRO_0000259549"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 76..124
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043201"
FT VAR_SEQ 759..772
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_021463"
FT VAR_SEQ 773..792
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021464"
FT VARIANT 425
FT /note="H -> R (in dbSNP:rs17851788)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_028963"
FT CONFLICT 805
FT /note="K -> T (in Ref. 1; BAB14116)"
FT /evidence="ECO:0000305"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 38..54
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 58..73
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 116..128
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 153..167
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 170..185
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 191..197
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 208..224
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 228..244
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 249..262
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 266..282
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 289..300
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 306..319
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 323..327
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 344..350
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 357..373
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 379..392
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 403..422
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 428..437
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 442..445
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 446..456
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 461..477
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 486..500
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 507..517
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 523..536
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 540..550
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 554..556
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 557..575
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 584..605
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 610..612
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 616..640
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 646..649
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 650..652
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 659..661
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 667..692
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 697..719
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 743..759
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 762..766
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 768..770
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 773..784
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 793..795
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 802..804
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 823..825
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 831..833
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 835..839
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 841..843
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 849..860
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 862..867
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 871..874
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 879..881
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 884..886
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 888..890
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 902..907
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 924..926
FT /evidence="ECO:0007829|PDB:7CUN"
SQ SEQUENCE 962 AA; 106834 MW; 45253FE31FD5B96D CRC64;
MASNSTKSFL ADAGYGEQEL DANSALMELD KGLRSGKLGE QCEAVVRFPR LFQKYPFPIL
INSAFLKLAD VFRVGNNFLR LCVLKVTQQS EKHLEKILNV DEFVKRIFSV IHSNDPVARA
ITLRMLGSLA SIIPERKNAH HSIRQSLDSH DNVEVEAAVF AAANFSAQSK DFAVGICNKI
SEMIQGLATP VDLKLKLIPI LQHMHHDAIL ASSARQLLQQ LVTSYPSTKM VIVSLHTFTL
LAASSLVDTP KQIQLLLQYL KNDPRKAVKR LAIQDLKLLA NKTPHTWSRE NIQALCECAL
QTPYDSLKLG MLSVLSTLSG TIAIKHYFSI VPGNVSSSPR SSDLVKLAQE CCYHNNRGIA
AHGVRVLTNI TVSCQEKDLL ALEQDAVFGL ESLLVLCSQD DSPGAQATLK IALNCMVKLA
KGRPHLSQSV VETLLTQLHS AQDAARILMC HCLAAIAMQL PVLGDGMLGD LMELYKVIGR
SATDKQQELL VSLATVIFVA SQKALSVESK AVIKQQLESV SNGWTVYRIA RQASRMGNHD
MAKELYQSLL TQVASEHFYF WLNSLKEFSH AEQCLTGLQE ENYSSALSCI AESLKFYHKG
IASLTAASTP LNPLSFQCEF VKLRIDLLQA FSQLICTCNS LKTSPPPAIA TTIAMTLGND
LQRCGRISNQ MKQSMEEFRS LASRYGDLYQ ASFDADSATL RNVELQQQSC LLISHAIEAL
ILDPESASFQ EYGSTGTAHA DSEYERRMMS VYNHVLEEVE SLNRKYTPVS YMHTACLCNA
IIALLKVPLS FQRYFFQKLQ STSIKLALSP SPRNPAEPIA VQNNQQLALK VEGVVQHGSK
PGLFRKIQSV CLNVSSTLQS KSGQDYKIPI DNMTNEMEQR VEPHNDYFST QFLLNFAILG
THNITVESSV KDANGIVWKT GPRTTIFVKS LEDPYSQQIR LQQQQAQQPL QQQQQRNAYT
RF
