ID Q6ZWL1_HUMAN Unreviewed; 279 AA. AC Q6ZWL1; A6NCM2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 22-FEB-2023, entry version 100. DE SubName: Full=cDNA FLJ16017 fis, clone TESTI2002618, weakly similar to ADAM 2 {ECO:0000313|EMBL:BAC85489.1}; 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 {ECO:0000313|EMBL:BAC85489.1}; RN [1] {ECO:0000313|EMBL:BAC85489.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Testis {ECO:0000313|EMBL:BAC85489.1}; RA Suzuki O., Sasaki N., Aotsuka S., Shoji T., Ichihara T., Shiohata N., RA Matsumoto K., Hirano M., Sano S., Nomura R., Yoshikawa Y., Matsumura Y., RA Moriya S., Chiba E., Momiyama H., Onogawa S., Kaeriyama S., Satoh N., RA Matsunawa H., Takahashi E., Kataoka R., Kuga N., Kuroda A., Satoh I., RA Kamata K., Takami S., Terashima Y., Watanabe M., Sugiyama T., Irie R., RA Otsuki T., Sato H., Wakamatsu A., Ishii S., Yamamoto J., Isono Y., RA Kawai-Hio Y., Saito K., Nishikawa T., Kimura K., Yamashita H., Matsuo K., RA Nakamura Y., Sekine M., Kikuchi H., Kanda K., Wagatsuma M., Murakawa K., RA Kanehori K., Takahashi-Fujii A., Oshima A., Sugiyama A., Kawakami B., RA Suzuki Y., Sugano S., Nagahari K., Masuho Y., Nagai K., Isogai T.; RT "NEDO human cDNA sequencing project."; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. 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; AK122608; BAC85489.1; -; mRNA. DR AlphaFoldDB; Q6ZWL1; -. DR PeptideAtlas; Q6ZWL1; -. DR ProteomicsDB; 68493; -. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1. DR PANTHER; PTHR11905:SF24; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 32; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. PE 2: Evidence at transcript level; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..16 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 17..279 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004282942" FT DOMAIN 186..252 FT /note="Peptidase M12B" FT /evidence="ECO:0000259|PROSITE:PS50215" SQ SEQUENCE 279 AA; 32092 MW; 02630EBBB7153321 CRC64; MFRLWLLLAG LCGLLASRPG FQNSLLQIVI PEKIQTNTND SSEIEYEQIS YIIPIDEKLY TVHLKQRYFL ADNFMIYLYN QGSMNTYSSD IQTQCYYQGN IEGYPDSMVT LSTCSGLRGI LQFENVSYGI EPLESAVEFQ HVLYKLKNED NDIAIFIDRS LKEQPMDDNI FISEKSEPAV PDLFPLYLEM HIVVDKTLYD YWGSDSMIVT NKVIEIVGLA NSMFTQFKVT IVLSSLELWS DENKISTVGE ADWREMKSVI VVLRLNVDLQ AVVIFELVY //