ID ATRIP_HUMAN Reviewed; 791 AA. AC Q8WXE1; A8K6A3; A8K714; B2RCE7; B4DU92; B5MEB7; Q69YK9; Q8NHQ2; Q8WUG7; AC Q96CL3; Q9HA30; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 07-OCT-2020, entry version 161. DE RecName: Full=ATR-interacting protein; DE AltName: Full=ATM and Rad3-related-interacting protein; GN Name=ATRIP; Synonyms=AGS1; 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 147-160 AND RP 722-733, IDENTIFICATION BY MASS SPECTROMETRY, ALTERNATIVE SPLICING, RP PHOSPHORYLATION, INTERACTION WITH ATR, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=11721054; DOI=10.1126/science.1065521; RA Cortez D., Guntuku S., Qin J., Elledge S.J.; RT "ATR and ATRIP: partners in checkpoint signaling."; RL Science 294:1713-1716(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4). RC TISSUE=Endothelial cell, Fetal brain, Placenta, and Prostate; 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 GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Colon, Lymph, and Testis; 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 134-791 (ISOFORM 1). RC TISSUE=Melanoma; 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 [7] RP FUNCTION, AND INTERACTION WITH THE RPA COMPLEX. RX PubMed=12791985; DOI=10.1126/science.1083430; RA Zou L., Elledge S.J.; RT "Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes."; RL Science 300:1542-1548(2003). RN [8] RP DOMAIN, AND MUTAGENESIS OF 769-GLU-GLU-770 AND 774-ASP-ASP-775. RX PubMed=15758953; DOI=10.1038/nature03442; RA Falck J., Coates J., Jackson S.P.; RT "Conserved modes of recruitment of ATM, ATR and DNA-PKcs to sites of DNA RT damage."; RL Nature 434:605-611(2005). RN [9] RP INTERACTION WITH CEP164, AND SUBCELLULAR LOCATION. RX PubMed=18283122; DOI=10.1101/gad.1627708; RA Sivasubramaniam S., Sun X., Pan Y.R., Wang S., Lee E.Y.; RT "Cep164 is a mediator protein required for the maintenance of genomic RT stability through modulation of MDC1, RPA, and CHK1."; RL Genes Dev. 22:587-600(2008). RN [10] RP INTERACTION WITH CINP. RX PubMed=19889979; DOI=10.1073/pnas.0909345106; RA Lovejoy C.A., Xu X., Bansbach C.E., Glick G.G., Zhao R., Ye F., Sirbu B.M., RA Titus L.C., Shyr Y., Cortez D.; RT "Functional genomic screens identify CINP as a genome maintenance RT protein."; RL Proc. Natl. Acad. Sci. U.S.A. 106:19304-19309(2009). CC -!- FUNCTION: Required for checkpoint signaling after DNA damage. Required CC for ATR expression, possibly by stabilizing the protein. CC {ECO:0000269|PubMed:12791985}. CC -!- SUBUNIT: Interacts with ATR (By similarity). Heterodimer with ATR. The CC heterodimer binds the RPA complex and is then recruited to single- CC stranded DNA. Interacts with CEP164 (via N-terminus). Interacts with CC CINP. {ECO:0000250, ECO:0000269|PubMed:11721054, CC ECO:0000269|PubMed:12791985, ECO:0000269|PubMed:18283122, CC ECO:0000269|PubMed:19889979}. CC -!- INTERACTION: CC Q8WXE1; Q13535: ATR; NbExp=4; IntAct=EBI-747353, EBI-968983; CC Q8WXE1; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-747353, EBI-946029; CC Q8WXE1; Q9BUN5: CCDC28B; NbExp=3; IntAct=EBI-747353, EBI-10299032; CC Q8WXE1; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-747353, EBI-396137; CC Q8WXE1; P50750: CDK9; NbExp=3; IntAct=EBI-747353, EBI-1383449; CC Q8WXE1; Q9BW66: CINP; NbExp=9; IntAct=EBI-747353, EBI-739784; CC Q8WXE1; Q8NDB6: FAM156A; NbExp=3; IntAct=EBI-747353, EBI-749727; CC Q8WXE1; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-747353, EBI-739832; CC Q8WXE1; Q8WXB1: METTL21A; NbExp=3; IntAct=EBI-747353, EBI-8652459; CC Q8WXE1; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-747353, EBI-10172526; CC Q8WXE1; P00540: MOS; NbExp=3; IntAct=EBI-747353, EBI-1757866; CC Q8WXE1; P20592: MX2; NbExp=3; IntAct=EBI-747353, EBI-10200618; CC Q8WXE1; Q9BRL4: PCTK1; NbExp=3; IntAct=EBI-747353, EBI-10296950; CC Q8WXE1; O15160: POLR1C; NbExp=3; IntAct=EBI-747353, EBI-1055079; CC Q8WXE1; P13521: SCG2; NbExp=3; IntAct=EBI-747353, EBI-947132; CC Q8WXE1; O43597: SPRY2; NbExp=3; IntAct=EBI-747353, EBI-742487; CC Q8WXE1; Q5VWN6-2: TASOR2; NbExp=3; IntAct=EBI-747353, EBI-10172380; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11721054, CC ECO:0000269|PubMed:18283122}. Note=Redistributes to discrete nuclear CC foci upon DNA damage. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8WXE1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WXE1-2; Sequence=VSP_010504; CC Name=3; CC IsoId=Q8WXE1-3; Sequence=VSP_010501; CC Name=4; CC IsoId=Q8WXE1-5; Sequence=VSP_047011; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11721054}. CC -!- DOMAIN: The EEXXXDDL motif is required for the interaction with CC catalytic subunit PRKDC and its recruitment to sites of DNA damage. CC {ECO:0000269|PubMed:15758953}. CC -!- PTM: Phosphorylated by ATR. {ECO:0000269|PubMed:11721054}. CC -!- SIMILARITY: Belongs to the ATRIP family. {ECO:0000305}. CC -!- CAUTION: The gene for this protein is either identical to or adjacent CC to that of TREX1. Some of the mRNAs that encode ATRIP also encode TREX1 CC in another reading frame. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB14029.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB14029.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAF84257.1; Type=Erroneous initiation; 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; AF451323; AAL38042.1; -; mRNA. DR EMBL; AK022405; BAB14029.1; ALT_SEQ; mRNA. DR EMBL; AK291568; BAF84257.1; ALT_INIT; mRNA. DR EMBL; AK291829; BAF84518.1; -; mRNA. DR EMBL; AK315075; BAG37544.1; -; mRNA. DR EMBL; AK300548; BAG62254.1; -; mRNA. DR EMBL; AC104448; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW64876.1; -; Genomic_DNA. DR EMBL; CH471055; EAW64878.1; -; Genomic_DNA. DR EMBL; BC014153; AAH14153.2; -; mRNA. DR EMBL; BC020563; AAH20563.1; -; mRNA. DR EMBL; BC030597; AAH30597.1; -; mRNA. DR EMBL; AL832917; CAH10621.1; -; mRNA. DR CCDS; CCDS2767.1; -. [Q8WXE1-2] DR CCDS; CCDS2768.1; -. [Q8WXE1-1] DR CCDS; CCDS59449.1; -. [Q8WXE1-3] DR CCDS; CCDS59450.1; -. [Q8WXE1-5] DR RefSeq; NP_001257951.1; NM_001271022.1. [Q8WXE1-5] DR RefSeq; NP_001257952.1; NM_001271023.1. [Q8WXE1-3] DR RefSeq; NP_115542.2; NM_032166.3. [Q8WXE1-2] DR RefSeq; NP_569055.1; NM_130384.2. [Q8WXE1-1] DR PDB; 4IGK; X-ray; 1.75 A; C/D=237-243. DR PDB; 4NB3; X-ray; 1.35 A; C/D=54-67. DR PDB; 5YZ0; EM; 4.70 A; C/D=1-791. DR PDBsum; 4IGK; -. DR PDBsum; 4NB3; -. DR PDBsum; 5YZ0; -. DR SMR; Q8WXE1; -. DR BioGRID; 313463; 64. DR ComplexPortal; CPX-3622; ATR-ATRIP DNA damage-sensing kinase complex. DR CORUM; Q8WXE1; -. DR DIP; DIP-46495N; -. DR ELM; Q8WXE1; -. DR IntAct; Q8WXE1; 37. DR MINT; Q8WXE1; -. DR STRING; 9606.ENSP00000323099; -. DR ChEMBL; CHEMBL4106138; -. DR iPTMnet; Q8WXE1; -. DR PhosphoSitePlus; Q8WXE1; -. DR BioMuta; ATRIP; -. DR DMDM; 48428109; -. DR CPTAC; CPTAC-3216; -. DR CPTAC; CPTAC-3217; -. DR CPTAC; CPTAC-914; -. DR CPTAC; CPTAC-915; -. DR EPD; Q8WXE1; -. DR jPOST; Q8WXE1; -. DR MassIVE; Q8WXE1; -. DR MaxQB; Q8WXE1; -. DR PaxDb; Q8WXE1; -. DR PeptideAtlas; Q8WXE1; -. DR PRIDE; Q8WXE1; -. DR ProteomicsDB; 6227; -. DR ProteomicsDB; 75018; -. [Q8WXE1-1] DR ProteomicsDB; 75019; -. [Q8WXE1-2] DR ProteomicsDB; 75020; -. [Q8WXE1-3] DR Antibodypedia; 30090; 542 antibodies. DR CPTC; Q8WXE1; 2 antibodies. DR DNASU; 84126; -. DR Ensembl; ENST00000320211; ENSP00000323099; ENSG00000164053. [Q8WXE1-1] DR Ensembl; ENST00000346691; ENSP00000302338; ENSG00000164053. [Q8WXE1-2] DR Ensembl; ENST00000357105; ENSP00000349620; ENSG00000164053. [Q8WXE1-5] DR Ensembl; ENST00000412052; ENSP00000400930; ENSG00000164053. [Q8WXE1-3] DR GeneID; 84126; -. DR KEGG; hsa:84126; -. DR UCSC; uc003ctf.3; human. [Q8WXE1-1] DR CTD; 84126; -. DR DisGeNET; 84126; -. DR EuPathDB; HostDB:ENSG00000164053.18; -. DR EuPathDB; HostDB:ENSG00000282827.1; -. DR GeneCards; ATRIP; -. DR HGNC; HGNC:33499; ATRIP. DR HPA; ENSG00000164053; Tissue enhanced (testis). DR MalaCards; ATRIP; -. DR MIM; 606605; gene. DR neXtProt; NX_Q8WXE1; -. DR OpenTargets; ENSG00000164053; -. DR Orphanet; 808; Seckel syndrome. DR PharmGKB; PA162377290; -. DR eggNOG; ENOG502QQF4; Eukaryota. DR GeneTree; ENSGT00390000012850; -. DR HOGENOM; CLU_024109_0_0_1; -. DR InParanoid; Q8WXE1; -. DR KO; K10905; -. DR OMA; TGSDCQC; -. DR PhylomeDB; Q8WXE1; -. DR TreeFam; TF324417; -. DR PathwayCommons; Q8WXE1; -. DR Reactome; R-HSA-176187; Activation of ATR in response to replication stress. DR Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA). DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends. DR Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange. DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway. DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation. DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint. DR SIGNOR; Q8WXE1; -. DR BioGRID-ORCS; 84126; 501 hits in 877 CRISPR screens. DR ChiTaRS; ATRIP; human. DR GenomeRNAi; 84126; -. DR Pharos; Q8WXE1; Tbio. DR PRO; PR:Q8WXE1; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q8WXE1; protein. DR Bgee; ENSG00000164053; Expressed in testis and 116 other tissues. DR ExpressionAtlas; Q8WXE1; baseline and differential. DR Genevisible; Q8WXE1; HS. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB. DR GO; GO:0000077; P:DNA damage checkpoint; IBA:GO_Central. DR GO; GO:0006281; P:DNA repair; IBA:GO_Central. DR GO; GO:0006260; P:DNA replication; TAS:Reactome. DR GO; GO:0036297; P:interstrand cross-link repair; TAS:Reactome. DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome. DR InterPro; IPR033349; ATRIP. DR PANTHER; PTHR28594; PTHR28594; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Coiled coil; Direct protein sequencing; KW DNA damage; DNA repair; Nucleus; Phosphoprotein; Polymorphism; KW Reference proteome. FT CHAIN 1..791 FT /note="ATR-interacting protein" FT /id="PRO_0000064740" FT REGION 118..156 FT /note="Interaction with CINP" FT /evidence="ECO:0000269|PubMed:19889979" FT COILED 108..217 FT /evidence="ECO:0000255" FT MOTIF 769..776 FT /note="EEXXXDL motif" FT VAR_SEQ 1..127 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_047011" FT VAR_SEQ 1..93 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_010501" FT VAR_SEQ 661..687 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_010504" FT VARIANT 125 FT /note="K -> Q (in dbSNP:rs11925638)" FT /id="VAR_050683" FT VARIANT 240 FT /note="P -> L (in dbSNP:rs35240314)" FT /id="VAR_050684" FT MUTAGEN 769..770 FT /note="EE->AA: Abolishes interaction with ATR and its FT recruitment to sites of DNA damage." FT /evidence="ECO:0000269|PubMed:15758953" FT MUTAGEN 774..775 FT /note="DD->AA: Abolishes interaction with ATR and its FT recruitment to sites of DNA damage." FT /evidence="ECO:0000269|PubMed:15758953" FT CONFLICT 280 FT /note="P -> L (in Ref. 5; AAH14153)" FT /evidence="ECO:0000305" FT CONFLICT 343 FT /note="T -> A (in Ref. 2; BAF84257)" FT /evidence="ECO:0000305" FT CONFLICT 492 FT /note="V -> I (in Ref. 2; BAF84257)" FT /evidence="ECO:0000305" FT CONFLICT 647 FT /note="A -> T (in Ref. 2; BAG62254)" FT /evidence="ECO:0000305" FT CONFLICT 683 FT /note="N -> D (in Ref. 2; BAF84257)" FT /evidence="ECO:0000305" FT CONFLICT 687 FT /note="V -> I (in Ref. 5; AAH30597)" FT /evidence="ECO:0000305" FT CONFLICT 712 FT /note="Q -> K (in Ref. 2; BAF84257)" FT /evidence="ECO:0000305" FT CONFLICT 777 FT /note="C -> G (in Ref. 2; BAF84257)" FT /evidence="ECO:0000305" FT HELIX 57..63 FT /evidence="ECO:0000244|PDB:4NB3" SQ SEQUENCE 791 AA; 85838 MW; 58981602F7961756 CRC64; MAGTSAPGSK RRSEPPAPRP GPPPGTGHPP SKRARGFSAA AAPDPDDPFG AHGDFTADDL EELDTLASQA LSQCPAAARD VSSDHKVHRL LDGMSKNPSG KNRETVPIKD NFELEVLQAQ YKELKEKMKV MEEEVLIKNG EIKILRDSLH QTESVLEEQR RSHFLLEQEK TQALSDKEKE FSKKLQSLQS ELQFKDAEMN ELRTKLQTSE RANKLAAPSV SHVSPRKNPS VVIKPEACSP QFGKTSFPTK ESFSANMSLP HPCQTESGYK PLVGREDSKP HSLRGDSIKQ EEAQKSFVDS WRQRSNTQGS ILINLLLKQP LIPGSSLSLC HLLSSSSESP AGTPLQPPGF GSTLAGMSGL RTTGSYDGSF SLSALREAQN LAFTGLNLVA RNECSRDGDP AEGGRRAFPL CQLPGAVHFL PLVQFFIGLH CQALQDLAAA KRSGAPGDSP THSSCVSSGV ETNPEDSVCI LEGFSVTALS ILQHLVCHSG AVVSLLLSGV GADSAAGEGN RSLVHRLSDG DMTSALRGVA DDQGQHPLLK MLLHLLAFSS AATGHLQASV LTQCLKVLVK LAENTSCDFL PRFQCVFQVL PKCLSPETPL PSVLLAVELL SLLADHDQLA PQLCSHSEGC LLLLLYMYIT SRPDRVALET QWLQLEQEVV WLLAKLGVQS PLPPVTGSNC QCNVEVVRAL TVMLHRQWLT VRRAGGPPRT DQQRRTVRCL RDTVLLLHGL SQKDKLFMMH CVEVLHQFDQ VMPGVSMLIR GLPDVTDCEE AALDDLCAAE TDVEDPEVEC G //