RPA2_HUMAN
ID RPA2_HUMAN Reviewed; 1135 AA.
AC Q9H9Y6; B7Z6Y7; B7Z823; F5GZX4; F8W898; Q2TAM4; Q585T5; Q6ZRR2; Q9H9D3;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA2;
DE Short=RNA polymerase I subunit 2;
DE EC=2.7.7.6 {ECO:0000305|PubMed:16809778};
DE AltName: Full=DNA-directed RNA polymerase I 135 kDa polypeptide;
DE Short=RPA135;
GN Name=POLR1B;
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; 2; 3 AND 4), AND
RP VARIANTS LEU-295 AND ARG-887 (ISOFORM 4).
RC TISSUE=Spleen, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT LEU-295.
RC TISSUE=Pancreas;
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 SUBCELLULAR LOCATION.
RX PubMed=11250903; DOI=10.1093/emboj/20.6.1373;
RA Miller G., Panov K.I., Friedrich J.K., Trinkle-Mulcahy L., Lamond A.I.,
RA Zomerdijk J.C.B.M.;
RT "hRRN3 is essential in the SL1-mediated recruitment of RNA polymerase I to
RT rRNA gene promoters.";
RL EMBO J. 20:1373-1382(2001).
RN [5]
RP IDENTIFICATION IN THE RNA POL I COMPLEX, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16809778; DOI=10.1128/mcb.00230-06;
RA Panov K.I., Panova T.B., Gadal O., Nishiyama K., Saito T., Russell J.,
RA Zomerdijk J.C.B.M.;
RT "RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation
RT of transcription by upstream binding factor.";
RL Mol. Cell. Biol. 26:5436-5448(2006).
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-1051, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [8]
RP INVOLVEMENT IN TCS4, AND VARIANTS TCS4 ARG-682; CYS-1003 AND SER-1003.
RX PubMed=31649276; DOI=10.1038/s41436-019-0669-9;
RA Sanchez E., Laplace-Builhe B., Mau-Them F.T., Richard E., Goldenberg A.,
RA Toler T.L., Guignard T., Gatinois V., Vincent M., Blanchet C., Boland A.,
RA Bihoreau M.T., Deleuze J.F., Olaso R., Nephi W., Luedecke H.J.,
RA Verheij J.B.G.M., Moreau-Lenoir F., Denoyelle F., Riviere J.B.,
RA Laplanche J.L., Willing M., Captier G., Apparailly F., Wieczorek D.,
RA Collet C., Djouad F., Genevieve D.;
RT "POLR1B and neural crest cell anomalies in Treacher Collins syndrome type
RT 4.";
RL Genet. Med. 22:547-556(2020).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Second largest core component of RNA polymerase I which synthesizes
CC ribosomal RNA precursors. Proposed to contribute to the polymerase
CC catalytic activity and forms the polymerase active center together with
CC the largest subunit. Pol I is composed of mobile elements and RPA2 is
CC part of the core element with the central large cleft and probably a
CC clamp element that moves to open and close the cleft.
CC {ECO:0000305|PubMed:16809778}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000305|PubMed:16809778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249;
CC Evidence={ECO:0000305|PubMed:16809778};
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of at least 13 subunits. {ECO:0000269|PubMed:16809778}.
CC -!- INTERACTION:
CC Q9H9Y6; O95602: POLR1A; NbExp=3; IntAct=EBI-355441, EBI-359472;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11250903}.
CC Chromosome {ECO:0000250|UniProtKB:P70700}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9H9Y6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H9Y6-2; Sequence=VSP_017823;
CC Name=3;
CC IsoId=Q9H9Y6-3; Sequence=VSP_056750;
CC Name=4;
CC IsoId=Q9H9Y6-4; Sequence=VSP_056749;
CC Name=5;
CC IsoId=Q9H9Y6-5; Sequence=VSP_056751;
CC -!- DISEASE: Treacher Collins syndrome 4 (TCS4) [MIM:618939]: A form of
CC Treacher Collins syndrome, a disorder of craniofacial development.
CC Treacher Collins syndrome is characterized by a combination of
CC bilateral downward slanting of the palpebral fissures, colobomas of the
CC lower eyelids with a paucity of eyelashes medial to the defect,
CC hypoplasia of the facial bones, cleft palate, malformation of the
CC external ears, atresia of the external auditory canals, and bilateral
CC conductive hearing loss. TCS4 inheritance pattern is autosomal
CC dominant. {ECO:0000269|PubMed:31649276}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
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DR EMBL; AK022533; BAB14082.1; -; mRNA.
DR EMBL; AK022890; BAB14296.1; -; mRNA.
DR EMBL; AK128044; BAC87247.1; -; mRNA.
DR EMBL; AK301178; BAH13423.1; -; mRNA.
DR EMBL; AK302814; BAH13809.1; -; mRNA.
DR EMBL; AC012442; AAX81999.1; -; Genomic_DNA.
DR EMBL; BC110833; AAI10834.1; -; mRNA.
DR CCDS; CCDS2097.1; -. [Q9H9Y6-1]
DR CCDS; CCDS46395.1; -. [Q9H9Y6-2]
DR CCDS; CCDS62988.1; -. [Q9H9Y6-3]
DR CCDS; CCDS62989.1; -. [Q9H9Y6-5]
DR CCDS; CCDS62990.1; -. [Q9H9Y6-4]
DR RefSeq; NP_001131076.1; NM_001137604.2. [Q9H9Y6-2]
DR RefSeq; NP_001269701.1; NM_001282772.1. [Q9H9Y6-3]
DR RefSeq; NP_001269703.1; NM_001282774.1. [Q9H9Y6-5]
DR RefSeq; NP_001269705.1; NM_001282776.1. [Q9H9Y6-4]
DR RefSeq; NP_001269706.1; NM_001282777.1.
DR RefSeq; NP_001269708.1; NM_001282779.1.
DR RefSeq; NP_061887.2; NM_019014.5. [Q9H9Y6-1]
DR PDB; 7OB9; EM; 2.70 A; B=1-1135.
DR PDB; 7OBA; EM; 3.10 A; B=1-1135.
DR PDB; 7OBB; EM; 3.30 A; B=1-1135.
DR PDB; 7VBA; EM; 2.89 A; B=1-1135.
DR PDB; 7VBB; EM; 2.81 A; B=1-1135.
DR PDB; 7VBC; EM; 3.01 A; B=1-1135.
DR PDBsum; 7OB9; -.
DR PDBsum; 7OBA; -.
DR PDBsum; 7OBB; -.
DR PDBsum; 7VBA; -.
DR PDBsum; 7VBB; -.
DR PDBsum; 7VBC; -.
DR AlphaFoldDB; Q9H9Y6; -.
DR SMR; Q9H9Y6; -.
DR BioGRID; 123926; 131.
DR CORUM; Q9H9Y6; -.
DR DIP; DIP-27538N; -.
DR IntAct; Q9H9Y6; 36.
DR MINT; Q9H9Y6; -.
DR STRING; 9606.ENSP00000444136; -.
DR GlyGen; Q9H9Y6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H9Y6; -.
DR PhosphoSitePlus; Q9H9Y6; -.
DR BioMuta; POLR1B; -.
DR DMDM; 92090637; -.
DR SWISS-2DPAGE; Q9H9Y6; -.
DR EPD; Q9H9Y6; -.
DR jPOST; Q9H9Y6; -.
DR MassIVE; Q9H9Y6; -.
DR MaxQB; Q9H9Y6; -.
DR PaxDb; Q9H9Y6; -.
DR PeptideAtlas; Q9H9Y6; -.
DR PRIDE; Q9H9Y6; -.
DR ProteomicsDB; 25159; -.
DR ProteomicsDB; 30108; -.
DR ProteomicsDB; 81369; -. [Q9H9Y6-1]
DR ProteomicsDB; 81370; -. [Q9H9Y6-2]
DR Antibodypedia; 18109; 127 antibodies from 24 providers.
DR DNASU; 84172; -.
DR Ensembl; ENST00000263331.10; ENSP00000263331.5; ENSG00000125630.16. [Q9H9Y6-1]
DR Ensembl; ENST00000409894.7; ENSP00000387143.3; ENSG00000125630.16. [Q9H9Y6-5]
DR Ensembl; ENST00000417433.6; ENSP00000405358.2; ENSG00000125630.16. [Q9H9Y6-2]
DR Ensembl; ENST00000537335.5; ENSP00000437914.1; ENSG00000125630.16. [Q9H9Y6-4]
DR Ensembl; ENST00000541869.5; ENSP00000444136.1; ENSG00000125630.16. [Q9H9Y6-3]
DR GeneID; 84172; -.
DR KEGG; hsa:84172; -.
DR MANE-Select; ENST00000263331.10; ENSP00000263331.5; NM_019014.6; NP_061887.2.
DR UCSC; uc002thw.4; human. [Q9H9Y6-1]
DR CTD; 84172; -.
DR DisGeNET; 84172; -.
DR GeneCards; POLR1B; -.
DR GeneReviews; POLR1B; -.
DR HGNC; HGNC:20454; POLR1B.
DR HPA; ENSG00000125630; Low tissue specificity.
DR MalaCards; POLR1B; -.
DR MIM; 602000; gene.
DR MIM; 618939; phenotype.
DR neXtProt; NX_Q9H9Y6; -.
DR OpenTargets; ENSG00000125630; -.
DR Orphanet; 861; Treacher-Collins syndrome.
DR PharmGKB; PA130601182; -.
DR VEuPathDB; HostDB:ENSG00000125630; -.
DR eggNOG; KOG0216; Eukaryota.
DR GeneTree; ENSGT00950000183132; -.
DR HOGENOM; CLU_000524_5_1_1; -.
DR InParanoid; Q9H9Y6; -.
DR OMA; FFGVVHY; -.
DR OrthoDB; 42570at2759; -.
DR PhylomeDB; Q9H9Y6; -.
DR TreeFam; TF103055; -.
DR PathwayCommons; Q9H9Y6; -.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
DR SignaLink; Q9H9Y6; -.
DR SIGNOR; Q9H9Y6; -.
DR BioGRID-ORCS; 84172; 782 hits in 1057 CRISPR screens.
DR ChiTaRS; POLR1B; human.
DR GeneWiki; POLR1B; -.
DR GenomeRNAi; 84172; -.
DR Pharos; Q9H9Y6; Tbio.
DR PRO; PR:Q9H9Y6; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9H9Y6; protein.
DR Bgee; ENSG00000125630; Expressed in buccal mucosa cell and 206 other tissues.
DR ExpressionAtlas; Q9H9Y6; baseline and differential.
DR Genevisible; Q9H9Y6; HS.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0014029; P:neural crest formation; ISS:UniProtKB.
DR GO; GO:0017126; P:nucleologenesis; IEA:Ensembl.
DR GO; GO:0009303; P:rRNA transcription; IEA:Ensembl.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR InterPro; IPR009674; Rpa2_dom_4.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF06883; RNA_pol_Rpa2_4; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; Disease variant;
KW DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription; Transferase;
KW Zinc; Zinc-finger.
FT CHAIN 1..1135
FT /note="DNA-directed RNA polymerase I subunit RPA2"
FT /id="PRO_0000048072"
FT ZN_FING 1070..1101
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:P22138"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1051
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..211
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056749"
FT VAR_SEQ 1
FT /note="M -> MRAKEAAETGLRPLLPACTERLASGVYRETGVRCAGGHM (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056750"
FT VAR_SEQ 61..116
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017823"
FT VAR_SEQ 387..582
FT /note="EKLEGWLVSIKIAFDKKAQKTSVSMNTDNLMRIFTMGIDLTKPFEYLFATGN
FT LRSKTGLGLLQDSGLCVVADKLNFIRYLSHFRCVHRGADFAKMRTTTVRRLLPESWGFL
FT CPVHTPDGEPCGLMNHLTAVCEVVTQFVYTASIPALLCNLGVTPIDGAPHRSYSECYPV
FT LLDGVMVGWVDKDLAPGIADSLRHFK -> GSLPLMELPTDHT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056751"
FT VARIANT 295
FT /note="S -> L (in dbSNP:rs1545133)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034476"
FT VARIANT 682
FT /note="S -> R (in TCS4; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:31649276"
FT /id="VAR_084557"
FT VARIANT 887
FT /note="H -> R"
FT /id="VAR_071195"
FT VARIANT 1003
FT /note="R -> C (in TCS4)"
FT /evidence="ECO:0000269|PubMed:31649276"
FT /id="VAR_084558"
FT VARIANT 1003
FT /note="R -> S (in TCS4)"
FT /evidence="ECO:0000269|PubMed:31649276"
FT /id="VAR_084559"
FT CONFLICT 247
FT /note="L -> R (in Ref. 1; BAB14082)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="E -> G (in Ref. 3; AAI10834)"
FT /evidence="ECO:0000305"
FT CONFLICT 746
FT /note="I -> T (in Ref. 1; BAB14296)"
FT /evidence="ECO:0000305"
FT CONFLICT 800
FT /note="D -> G (in Ref. 1; BAC87247)"
FT /evidence="ECO:0000305"
FT CONFLICT 868
FT /note="C -> R (in Ref. 1; BAB14082)"
FT /evidence="ECO:0000305"
FT CONFLICT 889
FT /note="Q -> R (in Ref. 1; BAB14082)"
FT /evidence="ECO:0000305"
FT CONFLICT 1039
FT /note="E -> G (in Ref. 1; BAH13809)"
FT /evidence="ECO:0000305"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 22..25
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:7OBB"
FT HELIX 40..60
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 69..83
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 125..135
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:7OBA"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 201..216
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:7OBA"
FT STRAND 221..229
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 234..242
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 249..256
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 261..268
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 276..291
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 297..307
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 320..330
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 339..357
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 377..405
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 419..422
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 428..436
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 462..465
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 477..480
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 485..487
FT /evidence="ECO:0007829|PDB:7OBA"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 494..496
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 506..510
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 511..514
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 530..536
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 540..544
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 550..552
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 553..560
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 562..567
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 568..570
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 571..584
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 594..598
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 602..604
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 609..613
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 619..625
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 626..629
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 630..635
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 636..639
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 653..655
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 658..662
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 663..666
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 671..673
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 677..679
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 682..691
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 693..695
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 703..705
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 712..716
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 721..723
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 726..729
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 732..734
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 739..741
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 743..745
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 749..751
FT /evidence="ECO:0007829|PDB:7OBA"
FT STRAND 757..760
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 761..765
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 766..769
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 771..780
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 781..784
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 788..790
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 792..794
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 801..803
FT /evidence="ECO:0007829|PDB:7OBA"
FT TURN 804..806
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 811..813
FT /evidence="ECO:0007829|PDB:7OBA"
FT STRAND 823..830
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 831..833
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 836..840
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 847..855
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 858..860
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 866..873
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 882..884
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 886..888
FT /evidence="ECO:0007829|PDB:7OBA"
FT STRAND 890..897
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 899..901
FT /evidence="ECO:0007829|PDB:7OBA"
FT STRAND 905..908
FT /evidence="ECO:0007829|PDB:7OBA"
FT STRAND 912..915
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 917..919
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 921..923
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 927..941
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 954..956
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 958..968
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 975..977
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 982..984
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 992..994
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 997..1003
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1006..1008
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1011..1015
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 1020..1022
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 1029..1032
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1034..1037
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1039..1046
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 1047..1049
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1051..1059
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1065..1070
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 1071..1074
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1075..1081
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1088..1091
FT /evidence="ECO:0007829|PDB:7OBA"
FT STRAND 1096..1098
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 1099..1101
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1104..1112
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1114..1124
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 1125..1127
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1128..1135
FT /evidence="ECO:0007829|PDB:7OB9"
SQ SEQUENCE 1135 AA; 128229 MW; 1F019E07F866C22E CRC64;
MDPGSRWRNL PSGPSLKHLT DPSYGIPREQ QKAALQELTR AHVESFNYAV HEGLGLAVQA
IPPFEFAFKD ERISFTILDA VISPPTVPKG TICKEANVYP AECRGRRSTY RGKLTADINW
AVNGISKGII KQFLGYVPIM VKSKLCNLRN LPPQALIEHH EEAEEMGGYF IINGIEKVIR
MLIMPRRNFP IAMIRPKWKT RGPGYTQYGV SMHCVREEHS AVNMNLHYLE NGTVMLNFIY
RKELFFLPLG FALKALVSFS DYQIFQELIK GKEDDSFLRN SVSQMLRIVM EEGCSTQKQV
LNYLGECFRV KLNVPDWYPN EQAAEFLFNQ CICIHLKSNT EKFYMLCLMT RKLFALAKGE
CMEDNPDSLV NQEVLTPGQL FLMFLKEKLE GWLVSIKIAF DKKAQKTSVS MNTDNLMRIF
TMGIDLTKPF EYLFATGNLR SKTGLGLLQD SGLCVVADKL NFIRYLSHFR CVHRGADFAK
MRTTTVRRLL PESWGFLCPV HTPDGEPCGL MNHLTAVCEV VTQFVYTASI PALLCNLGVT
PIDGAPHRSY SECYPVLLDG VMVGWVDKDL APGIADSLRH FKVLREKRIP PWMEVVLIPM
TGKPSLYPGL FLFTTPCRLV RPVQNLALGK EELIGTMEQI FMNVAIFEDE VFAGVTTHQE
LFPHSLLSVI ANFIPFSDHN QSPRNMYQCQ MGKQTMGFPL LTYQDRSDNK LYRLQTPQSP
LVRPSMYDYY DMDNYPIGTN AIVAVISYTG YDMEDAMIVN KASWERGFAH GSVYKSEFID
LSEKIKQGDS SLVFGIKPGD PRVLQKLDDD GLPFIGAKLQ YGDPYYSYLN LNTGESFVMY
YKSKENCVVD NIKVCSNDTG SGKFKCVCIT MRVPRNPTIG DKFASRHGQK GILSRLWPAE
DMPFTESGMV PDILFNPHGF PSRMTIGMLI ESMAGKSAAL HGLCHDATPF IFSEENSALE
YFGEMLKAAG YNFYGTERLY SGISGLELEA DIFIGVVYYQ RLRHMVSDKF QVRTTGARDR
VTNQPIGGRN VQGGIRFGEM ERDALLAHGT SFLLHDRLFN CSDRSVAHVC VKCGSLLSPL
LEKPPPSWSA MRNRKYNCTL CSRSDTIDTV SVPYVFRYFV AELAAMNIKV KLDVV
