Lustrin　A　is　the　first　nacre　protein　with　specific　structure　and　amino　acid　residue　content　that　was　identified　in　abalone;　since　its　identification,　homologs　have　been　found　in　several　abalone　species.　In　this　study,　we　isolated　and　cloned　the　complete　cDNA　of　Lustrin　A　from　Haliotis　discus　hannai,　which　was　named　Hdh-Lustrin　A.　Hdh-Lustrin　A　has　characteristic　cysteine-　and　proline-rich　domains,　glycine-　and　serine-rich　domains,　and　a　whey　acidic　protein　(WAP)-like　C-terminus.　The　cysteine-　and　praline-rich　domains　showed　internal　similarity　repeats　that　arrayed　in　gene　coding　region,　and　the　phylogenetic　tree　of　these　repeats　indicated　that　the　similarity　of　structural　repetitive　unit　components　in　different　abalone　species,　reflecting　their　evolutionary　distance.　A　tissue　distribution　analysis　showed　that　the　mRNA　level　of　Hdh-Lustrin　A　has　tissue-specific　expression　in　mantle.　Under　lipopolysaccharide　(LPS)　challenge,　Hdh-Lustrin　A　showed　a　significantly　increase,　while　it　showed　a　more　complex　pattern　with　two　peaks　in　the　process　of　shell　regeneration.　Moreover,　acidification　and　warming　raised　the　expression　level　of　Hdh-Lustrin　A　in　shell　regeneration　in　two　different　manners;　acidification　raised　the　gene　expression　in　quick　response,　in　contrast　the　long　run　in　warming　treatment.　Similar　pattern　also　has　been　detected　in　immune　reaction　and　the　thermal　treatments.　These　results　suggest　that　the　Hdh-Lustrin　A　is　a　nacre　protein,　which　can　be　distinguished　by　its　cysteine-　and　proline-rich　domain.　It　involves　in　shell　regeneration　and　innate　immunity　in　abalone,　and　its　expression　pattern　during　shell　regeneration　can　be　disrupted　by　physicochemical　properties　of　the　environment.