ID K1QGP8_CRAGI Unreviewed; 2082 AA.
AC K1QGP8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Atrial natriuretic peptide-converting enzyme {ECO:0000313|EMBL:EKC33048.1};
GN ORFNames=CGI_10012458 {ECO:0000313|EMBL:EKC33048.1};
OS Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC33048.1};
RN [1] {ECO:0000313|EMBL:EKC33048.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC33048.1};
RX PubMed=22992520; DOI=10.1038/nature11413;
RA Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT "The oyster genome reveals stress adaptation and complexity of shell
RT formation.";
RL Nature 490:49-54(2012).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR EMBL; JH817406; EKC33048.1; -; Genomic_DNA.
DR HOGENOM; CLU_232653_0_0_1; -.
DR InParanoid; K1QGP8; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd07066; CRD_FZ; 7.
DR CDD; cd00112; LDLa; 6.
DR CDD; cd06263; MAM; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 8.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 6.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF7; HYALIN; 1.
DR Pfam; PF01392; Fz; 6.
DR Pfam; PF00057; Ldl_recept_a; 4.
DR Pfam; PF00629; MAM; 3.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00063; FRI; 2.
DR SMART; SM00192; LDLa; 7.
DR SMART; SM00137; MAM; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 8.
DR SUPFAM; SSF57424; LDL receptor-like module; 6.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50038; FZ; 8.
DR PROSITE; PS01209; LDLRA_1; 3.
DR PROSITE; PS50068; LDLRA_2; 6.
DR PROSITE; PS50060; MAM_2; 3.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}.
FT DISULFID 134..172
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 242..280
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 387..425
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 508..546
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 632..670
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 741..779
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 980..995
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 998..1010
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1005..1023
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1017..1032
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1798..1813
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1815..1827
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1822..1840
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2053..2071
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2065..2080
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 2082 AA; 229502 MW; BD683F5B66033F1D CRC64;
MQSCSDNAML YLCTIMYPSC DDQSLPCSDF CRSVQRECGN NFELAKPSYC DKLPSTDCVN
PEVTTTTTIQ TTTTSVTTPS TLPTPTTSPA LCLTLEIPEC QAVGHTSFMF PNFFGHNSVE
DAMAHLTFYK NQSCSASSMY YVCNMLFPKC DPATGLFIYA CQDHCNAVYT ACPSLTLAEP
SRCNILPTSN CEPKKEEELC LTLEIPECQA VGHTSVTFPN VFNHYSIEDA MSYFNSFKGK
SCSASSMYFL CNILFPKCDP ATGRMTYACQ DHCNDTYASC PYLQLASPNY CAALPTSQCE
PSYQSQVTTT QLVTTTQTVA TTPTQPVTTT TTPQPETTTT QPALCLTLEI PECQAVGHTC
VMLPNFFGQN SIQEAMAYFN FYKNQSCSAS SMYYLCNMLF PKCDPATGLL SYACQDHCTS
VSASCPGLSL ASSQYCSSLP FTSCVPIYQG PVTTTIQPET TPQPGCLSLQ IPECRDLGHT
SVMLPNAFGH NSLEQATTYF KVFKNESCSA SALYYICNML FPKCDPATKQ VIYPCQSHCR
DVLSSCPTLA MADNSYCVQL PTTSCEPSYQ DATTITTTQE PETTPQPELC YTTTVPECLA
VNQTHFLLPN AFGDMTLSAA VERFGYYKNE SCSAKFMLYL CNMFFPTCNT STGMMQFPCK
SLCNEANMEC PDMMLSGPSY CNSLPVTGCV GEETTQEVCE TINAPECRAI GLHYTQMPNV
FNHLDLATAK QFFDQFNQQS CSQRAVYYTC LMVFPMCDRI TGSQKYACQE DCYAINRECG
NATQLAGLAY CPSLPTVDSG NCHQIPLTTT PAPTTSVATT KTPGVCIPLS VPECQAVGRS
STMFPNLFGH TTLEDANTVF AIFKRDEFCS QNAMYYLCSL VYPVCSGGVR INPCQSYCDD
VQAECGTNFT AAINNYCDYL PLDQCVSGFP GVSTTQAPTT TTTQGLLTVP STLGPRENCS
ETNRYTCPSN GKCIMKEWVC DGEPDCEDQS DEVNCGSCSS DQFTCLDRSC VPAGERCNKV
PACPDESDER NCVSLTTQSI LQLSSRPLCY QSWSDSLGPE VCRSLGLGNF SNALSMQYFS
SQYVHLDMNG QVPSHLGKTS VRAECQGAMV VALKCEPRGC GQRLVGSSQV GFIVGGNDAV
PGYWPWQVSV QLKLPGGTTK HICGGSLVAP NFVLTATHCL SYLADRNVLI GATNRGVAEE
TQKQYEIKRV IKGLENFQQY GPGDITLFEL NDTVKYTPYI QPICFAEADE KFTETSICYA
TGWGYTTPGD KTYSTMLKEL KMRLWSTSKC NSTAHWNGNI TGGYLCAGYQ SNLKSVCTGD
SGGPLVCKNN QGIWKLVGIS SYVAINCSAQ NLPNVFTDVK HYLPWVKSEL ECKFKCDNGR
CLFDRGMVCN RKNDCGDNSD ETRLCEISVN CTFDDNYLCG YNASGFIWSY GASNSQAQSS
LPWTDHTIGH YPGHFMFGKF GTLPEASLMS PKFQISVQSC VRFYYLRRGY SNDNMIVRTW
EYSLSGIPIS NTAYVVGPDS SPDVWKLGYF DLSAGTYHLE FISTESHKTA LDDVKVVPGF
CSQSVCDANM YRCADDKANP VCLPQSSICN VVVECNKDEA NCQANTTKYT CDFEKAMHCG
ISQITDDRGE FLMMNGSYLR EKILYEEAFN EHTNNDSDAW MLFALTNLQY LVGNSVQMTQ
KLFLDNQLFC LSFYYRAQTD MTFKVSLESK GEVYDLLSFT DRSTFDWTKA QMQLPLVVSG
VLTYQLVRTF PPLNKYYKPY MAIDDISIIP GECPAYVCPE GTLKCASENF CYQSSQRCDR
ITNCPDETDE ANCTCTENEF SCQNGRCIPQ SSACDKKVDC LDKSDEGTVC DSLRSMTCTF
ETPFSCGYTS NEGLYTWQRH SGATPSFYTG PIADHTLGDT TGHYFFVEGN DGVRGEIAVL
TTPNVTTGVG QSLGFYYHII TENDFTFIQS EGLSVIAQLP DGRSQLLWWQ NQTSSYEWLY
GCVNLPDNTH LNIQFVTKRI GLDNQNNVFD ADVAVDDIAL LLLPCSEDAV TTEPVSSPAP
TVTPTVSDCA FRCDNGFCIK ADQRCNGMDE CRNGEDELNC PS
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