ID L5JZG5_PTEAL Unreviewed; 997 AA.
AC L5JZG5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Atrial natriuretic peptide-converting enzyme {ECO:0000313|EMBL:ELK03648.1};
GN ORFNames=PAL_GLEAN10016078 {ECO:0000313|EMBL:ELK03648.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK03648.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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; KB031078; ELK03648.1; -; Genomic_DNA.
DR AlphaFoldDB; L5JZG5; -.
DR STRING; 9402.L5JZG5; -.
DR eggNOG; KOG3577; Eukaryota.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; L5JZG5; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0016486; P:peptide hormone processing; IEA:InterPro.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:InterPro.
DR CDD; cd07445; CRD_corin_1; 1.
DR CDD; cd07888; CRD_corin_2; 1.
DR CDD; cd00112; LDLa; 7.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 2.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 7.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR017052; Corin.
DR InterPro; IPR041762; Corin_CRD_1.
DR InterPro; IPR041763; Corin_CRD_2.
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; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF7; HYALIN; 1.
DR Pfam; PF01392; Fz; 2.
DR Pfam; PF00057; Ldl_recept_a; 5.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF036376; Corin; 3.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00063; FRI; 2.
DR SMART; SM00192; LDLa; 7.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 2.
DR SUPFAM; SSF57424; LDL receptor-like module; 7.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50038; FZ; 2.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 114..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 202..327
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 482..605
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 783..997
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 284..308
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 345..363
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 357..372
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 374..386
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 381..399
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 393..408
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 418..436
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 430..445
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 455..473
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 467..482
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 534..572
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 561..602
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 565..589
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 612..624
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 619..637
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 631..646
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 669..684
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 687..699
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 694..712
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 706..721
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 997 AA; 111370 MW; F4B6F3406746C9A6 CRC64;
MRRVFFNVRV RSVQGPRSPW QGRCRICRVP SPPGALHASG GLCGTRAPGE AAEGAVGSSP
SGTLGFLSAP ASQTPGIWKD CAAALPAPDV LVSDEDNLND GCSQKLTTTN ILRFLLLVLI
PCICALIVLL VILLSFVGTL KKAHFKSNGS EPMATDGKNR TPDIILRNMI YNESEVTSAT
HPDQYMSAWT KNISLSRDQN HKNTSTCMNI THSQCQMLPY HTTLTSLFPI VKKMDMEKFL
KFFTYLHRLS CYQHIMLFGC SLAFPECVSD GDDSHGLLPC RSFCEAAREG CESILGMVNT
SWPDFLKCSQ FRSQTEISNV SRICFSPEQE KGKQSLCGGG ESFLCGSGTC IPRTLLCNGY
NDCDDWSDEA HCNCSENLFH CHTGKCLNYS LVCDGYDDCG DLSDEQNCDC NLTKEHRCGD
GRCIMMEWVC DGDHDCVDKS DEVNCSCHSQ GLMECGNGQC IPSSFQCDGD EDCKDRSDEE
GCSGSQCEPI TLELCMNLPY NHTYYPNYLG HRTQKEASIS WESSLFPALV QTNCYKYLMF
FACTILVPKC DVNTSQRIPP CRALCEQSKE RCESVLGIVG LQWPEGTDCN QFPEENSDNQ
TCLMPNEDVE ECSPSHFKCG SGRCVLASRR CNGEPDCDDD SDEENCGCKE RNLWECPTDK
QCLQHTVVCD GFPDCSDHMD EKNCSFCQDD ELECANHECV SRDQWCDGEA NCLDSSDEWD
CVSLSKNVDS FSFLTVYRSA TEHLVCGDGW QETLSQLACK QMGLGEPSVT ELIQEQKQDQ
QWLILHSNWK SLNGTTLHEL LVKGRETAAD WKVVFGINNL DHPSSYIQTR LVKTIILHPR
YSRAVVDYDI SIVELGEDIS ETSYVRPVCL PSMLQSLEPD TYCYITGWGH MGHKMPFKLQ
EGEVRVISLE QCQSYFDMKT ITTRMICAGY ESGTVDSCMI FIRSVASIIR SPSDLSYYLH
ALCSGCLRLS HPLHEERHLD QQQEENTIVL VYVTGPF
//
