ID LDH6B_HUMAN Reviewed; 381 AA. AC Q9BYZ2; Q6DUY4; Q96LI2; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 07-JUL-2009, entry version 73. DE RecName: Full=L-lactate dehydrogenase A-like 6B; DE EC=1.1.1.27; GN Name=LDHAL6B; Synonyms=LDHAL6, LDHL; 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]. RC TISSUE=Testis; RA Sha J.H., Li J.M., Zhou Z.M.; RT "A novel intronless human testis lactate dehydrogenase gene from adult RT testis."; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Tang W.W.; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS MET-14; LEU-30 RP AND THR-326. RC TISSUE=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., 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 MET-14; LEU-30 RP AND THR-326. RC TISSUE=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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH. CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)- CC lactate from pyruvate: step 1/1. CC -!- INTERACTION: CC Q14103:HNRNPD; NbExp=2; IntAct=EBI-1108377, EBI-299674; CC -!- TISSUE SPECIFICITY: Testis specific. CC -!- DEVELOPMENTAL STAGE: Higher expression level in adult testis as CC compared to 6-week-old fetal testis. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family. CC -!- CAUTION: It is uncertain whether Met-1 or Met-50 is the initiator. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY009108; AAG49399.1; -; mRNA. DR EMBL; AY642121; AAT65080.1; -; mRNA. DR EMBL; AK058192; BAB71710.1; -; mRNA. DR EMBL; BC022034; AAH22034.1; -; mRNA. DR IPI; IPI00016768; -. DR RefSeq; NP_149972.1; -. DR UniGene; Hs.307052; -. DR HSSP; P00338; 1I10. DR SMR; Q9BYZ2; 51-381. DR IntAct; Q9BYZ2; 1. DR PeptideAtlas; Q9BYZ2; -. DR PRIDE; Q9BYZ2; -. DR Ensembl; ENSG00000171989; Homo sapiens. DR GeneID; 92483; -. DR KEGG; hsa:92483; -. DR NMPDR; fig|9606.3.peg.10773; -. DR UCSC; uc002agb.1; human. DR GeneCards; GC15P057286; -. DR H-InvDB; HIX0012290; -. DR HGNC; HGNC:21481; LDHAL6B. DR PharmGKB; PA134943157; -. DR HOGENOM; Q9BYZ2; -. DR HOVERGEN; Q9BYZ2; -. DR OMA; Q9BYZ2; VHAYVLG. DR BRENDA; 1.1.1.27; 247. DR DrugBank; DB00157; NADH. DR NextBio; 77767; -. DR ArrayExpress; Q9BYZ2; -. DR Bgee; Q9BYZ2; -. DR CleanEx; HS_LDHAL6B; -. DR GermOnline; ENSG00000171989; Homo sapiens. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:EC. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0019642; P:anaerobic glycolysis; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR001557; L-lactate/malate_DH. DR InterPro; IPR011304; L-lactate_DH. DR InterPro; IPR018177; L-lactate_DH_AS. DR InterPro; IPR001236; Lactate/malate_DH. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 1. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR PRINTS; PR00086; LLDHDRGNASE. DR TIGRFAMs; TIGR01771; L-LDH-NAD; 1. DR PROSITE; PS00064; L_LDH; 1. PE 1: Evidence at protein level; KW Complete proteome; Glycolysis; NAD; Oxidoreductase; Polymorphism. FT CHAIN 1 381 L-lactate dehydrogenase A-like 6B. FT /FTId=PRO_0000168458. FT NP_BIND 101 106 NAD (By similarity). FT ACT_SITE 242 242 Proton acceptor (By similarity). FT BINDING 148 148 NAD (By similarity). FT BINDING 155 155 Substrate (By similarity). FT BINDING 187 187 NAD or substrate (By similarity). FT BINDING 218 218 Substrate (By similarity). FT BINDING 297 297 Substrate (By similarity). FT VARIANT 14 14 V -> M (in dbSNP:rs3809530). FT /FTId=VAR_027936. FT VARIANT 30 30 P -> L (in dbSNP:rs3809529). FT /FTId=VAR_027937. FT VARIANT 259 259 P -> S (in dbSNP:rs35212259). FT /FTId=VAR_049757. FT VARIANT 326 326 I -> T (in dbSNP:rs3825937). FT /FTId=VAR_027938. SQ SEQUENCE 381 AA; 41943 MW; F2B2D27E3ADE8A1D CRC64; MSWTVPVVRA SQRVSSVGAN FLCLGMALCP RQATRIPLNG TWLFTPVSKM ATVKSELIER FTSEKPVHHS KVSIIGTGSV GMACAISILL KGLSDELALV DLDEDKLKGE TMDLQHGSPF TKMPNIVCSK DYFVTANSNL VIITAGARQE KGETRLNLVQ RNVAIFKLMI SSIVQYSPHC KLIIVSNPVD ILTYVAWKLS AFPKNRIIGS GCNLDTARFR FLIGQKLGIH SESCHGWILG EHGDSSVPVW SGVNIAGVPL KDLNSDIGTD KDPEQWKNVH KEVTATAYEI IKMKGYTSWA IGLSVADLTE SILKNLRRIH PVSTIIKGLY GIDEEVFLSI PCILGENGIT NLIKIKLTPE EEAHLKKSAK TLWEIQNKLK L //