ID GLRX3_HUMAN Reviewed; 335 AA. AC O76003; Q96CE0; Q9P1B0; Q9P1B1; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 26-SEP-2003, sequence version 2. DT 22-JUL-2008, entry version 79. DE RecName: Full=Glutaredoxin-3; DE AltName: Full=Thioredoxin-like protein 2; DE AltName: Full=PKC-interacting cousin of thioredoxin; DE AltName: Full=PKC-theta-interacting protein; DE Short=PKCq-interacting protein; GN Name=GLRX3; Synonyms=PICOT, TXNL2; ORFNames=HUSSY-22; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH RP PKC-THETA, AND VARIANTS HIS-21 AND SER-123. RC TISSUE=Liver, Spleen, and T-cell lymphoma; RX MEDLINE=20102703; PubMed=10636891; DOI=10.1074/jbc.275.3.1902; RA Witte S., Villalba M., Bi K., Liu Y., Isakov N., Altman A.; RT "Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways RT by PICOT, a novel protein kinase C-interacting protein with a RT thioredoxin homology domain."; RL J. Biol. Chem. 275:1902-1909(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Melanocyte; RX MEDLINE=21064499; PubMed=11124703; RX DOI=10.1002/1097-0061(200101)18:1<69::AID-YEA647>3.3.CO;2-8; RA Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., RA Cannata N., Zimbello R., Lanfranchi G., Valle G.; RT "Characterization of 16 novel human genes showing high similarity to RT yeast sequences."; RL Yeast 18:69-80(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-21 AND RP SER-123. 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-21 AND RP SER-123. RC TISSUE=Bone marrow, and Urinary bladder; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP STRUCTURE BY NMR OF 1-119. RG RIKEN structural genomics initiative (RSGI); RT "The solution structure of the thioredoxin domain of human RT thioredoxin-like protein 2."; RL Submitted (APR-2007) to the PDB data bank. CC -!- FUNCTION: May play a role in regulating the function of the CC thioredoxin system. CC -!- SUBUNIT: Interacts weakly with PKC-theta. CC -!- INTERACTION: CC Q04759:PRKCQ; NbExp=2; IntAct=EBI-374781, EBI-374762; CC O76081:RGS20; NbExp=1; IntAct=EBI-374781, EBI-1052678; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Note=Under the CC plasma membrane. After PMA stimulation, GLRX3/TXNL2 and PRKCQ/PKC- CC theta translocate to a more extended submembrane area. CC -!- TISSUE SPECIFICITY: Expressed in heart, spleen, testis and, to a CC lower extent, in thymus and peripheral blood leukocytes. Weakly CC expressed in lung, placenta, colon and small intestine. CC -!- DOMAIN: The thioredoxin domain lacks the two redox-active CC cysteines. This strongly suggests that it lacks thioredoxin CC activity. CC -!- SIMILARITY: Contains 2 glutaredoxin domains. CC -!- SIMILARITY: Contains 1 thioredoxin domain. 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; AF118649; AAF28841.1; -; mRNA. DR EMBL; AF118652; AAF28844.1; -; mRNA. DR EMBL; AJ010841; CAA09375.1; -; mRNA. DR EMBL; AK022131; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK021926; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC005289; AAH05289.1; -; mRNA. DR EMBL; BC014372; AAH14372.2; -; mRNA. DR RefSeq; NP_006532.2; -. DR UniGene; Hs.42644; -. DR PDB; 2DIY; NMR; -; A=1-119. DR PDBsum; 2DIY; -. DR SMR; O76003; 239-335. DR IntAct; O76003; -. DR REPRODUCTION-2DPAGE; IPI00008552; -. DR PeptideAtlas; O76003; -. DR Ensembl; ENSG00000108010; Homo sapiens. DR GeneID; 10539; -. DR KEGG; hsa:10539; -. DR H-InvDB; HIX0009315; -. DR HGNC; HGNC:15987; GLRX3. DR PharmGKB; PA38075; -. DR HOGENOM; O76003; -. DR HOVERGEN; O76003; -. DR LinkHub; O76003; -. DR ArrayExpress; O76003; -. DR CleanEx; HS_GLRX3; -. DR GermOnline; ENSG00000108010; Homo sapiens. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR002109; Glutaredoxin. DR InterPro; IPR004480; Glutredox-rel. DR InterPro; IPR006662; Thioredoxin-like. DR InterPro; IPR013766; Thioredoxin_dom. DR InterPro; IPR012335; Thioredoxin_fold. DR Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 3. DR PANTHER; PTHR10293; Glutredox-rel; 1. DR Pfam; PF00462; Glutaredoxin; 2. DR Pfam; PF00085; Thioredoxin; 1. DR PRINTS; PR00421; THIOREDOXIN. DR TIGRFAMs; TIGR00365; Glutredox-rel; 2. DR PROSITE; PS51354; GLUTAREDOXIN_2; 2. DR PROSITE; PS00194; THIOREDOXIN_1; FALSE_NEG. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Polymorphism; Repeat. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 335 Glutaredoxin-3. FT /FTId=PRO_0000120019. FT DOMAIN 2 117 Thioredoxin. FT DOMAIN 144 236 Glutaredoxin 1. FT DOMAIN 237 335 Glutaredoxin 2. FT MOD_RES 2 2 N-acetylalanine (By similarity). FT VARIANT 21 21 Q -> H (in dbSNP:rs13991). FT /FTId=VAR_016875. FT VARIANT 123 123 P -> S (in dbSNP:rs2274217). FT /FTId=VAR_016876. FT CONFLICT 2 2 A -> E (in Ref. 2; CAA09375). FT CONFLICT 67 67 K -> R (in Ref. 3). FT CONFLICT 210 210 I -> T (in Ref. 3). FT STRAND 14 16 FT HELIX 19 28 FT STRAND 31 39 FT HELIX 45 59 FT STRAND 63 69 FT TURN 70 72 FT HELIX 74 80 FT STRAND 84 102 FT HELIX 105 116 SQ SEQUENCE 335 AA; 37432 MW; 46D644413D9EDFDA CRC64; MAAGAAEAAV AAVEEVGSAG QFEELLRLKA KSLLVVHFWA PWAPQCAQMN EVMAELAKEL PQVSFVKLEA EGVPEVSEKY EISSVPTFLF FKNSQKIDRL DGAHAPELTK KVQRHASSGS FLPSANEHLK EDLNLRLKKL THAAPCMLFM KGTPQEPRCG FSKQMVEILH KHNIQFSSFD IFSDEEVRQG LKAYSSWPTY PQLYVSGELI GGLDIIKELE ASEELDTICP KAPKLEERLK VLTNKASVML FMKGNKQEAK CGFSKQILEI LNSTGVEYET FDILEDEEVR QGLKAYSNWP TYPQLYVKGE LVGGLDIVKE LKENGELLPI LRGEN //