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Database: UniProt
Entry: H0Z4H6_TAEGU
LinkDB: H0Z4H6_TAEGU
Original site: H0Z4H6_TAEGU 
ID   H0Z4H6_TAEGU            Unreviewed;       521 AA.
AC   H0Z4H6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   24-JAN-2024, entry version 68.
DE   SubName: Full=Beta-secretase 2 {ECO:0000313|Ensembl:ENSTGUP00000005471.2};
GN   Name=BACE2 {ECO:0000313|Ensembl:ENSTGUP00000005471.2};
OS   Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC   Estrildinae; Taeniopygia.
OX   NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000005471.2, ECO:0000313|Proteomes:UP000007754};
RN   [1] {ECO:0000313|Ensembl:ENSTGUP00000005471.2, ECO:0000313|Proteomes:UP000007754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20360741; DOI=10.1038/nature08819;
RA   Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA   Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA   Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA   Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA   Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA   Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA   Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA   McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA   Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA   Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA   Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA   Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA   Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA   Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT   "The genome of a songbird.";
RL   Nature 464:757-762(2010).
RN   [2] {ECO:0000313|Ensembl:ENSTGUP00000005471.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   AlphaFoldDB; H0Z4H6; -.
DR   STRING; 59729.ENSTGUP00000005471; -.
DR   Ensembl; ENSTGUT00000005525.2; ENSTGUP00000005471.2; ENSTGUG00000005268.2.
DR   GeneTree; ENSGT00940000159548; -.
DR   HOGENOM; CLU_039009_0_0_1; -.
DR   InParanoid; H0Z4H6; -.
DR   OMA; KEWYYQV; -.
DR   OrthoDB; 603414at2759; -.
DR   TreeFam; TF329595; -.
DR   Proteomes; UP000007754; Chromosome 1.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0033162; C:melanosome membrane; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0032438; P:melanosome organization; IEA:Ensembl.
DR   GO; GO:0006509; P:membrane protein ectodomain proteolysis; IEA:Ensembl.
DR   GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; IEA:Ensembl.
DR   GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR   CDD; cd05473; beta_secretase_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR009119; BACE.
DR   InterPro; IPR009121; BACE2.
DR   InterPro; IPR033874; Memapsin-like.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47965; ASPARTYL PROTEASE-RELATED; 1.
DR   PANTHER; PTHR47965:SF40; BETA-SECRETASE 2; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR01817; BACE2.
DR   PRINTS; PR01815; BACEFAMILY.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR609121-2};
KW   Glycoprotein {ECO:0000256|PIRSR:PIRSR609121-3};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007754};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..521
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5025534195"
FT   TRANSMEM        470..495
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          95..432
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          39..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        113
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   CARBOHYD        369
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR609121-3"
FT   DISULFID        236..436
FT                   /evidence="ECO:0000256|PIRSR:PIRSR609121-2"
FT   DISULFID        295..460
FT                   /evidence="ECO:0000256|PIRSR:PIRSR609121-2"
FT   DISULFID        347..396
FT                   /evidence="ECO:0000256|PIRSR:PIRSR609121-2"
SQ   SEQUENCE   521 AA;  56257 MW;  5859385BFB92AB2E CRC64;
     MGTALAAPGL LLLLLLLAGT AGLCRALFSL PLRVSHPAAP AGSPPAPVVL RPASGSRQQD
     APGAADGLAL ASDPGGTLNF LAMVENLQGD SGRGYYLEML IGTPPQALNI LVDTGSSNFA
     VAGVPDPDVT SYFNPELSST YRSEGIEVTV KYSQGSWTGV LGTDVITMPK GLYGSYTINI
     ATILESENFF LPGVKWHGIL GLAYDALAKP SSSVETFFDS LVKQAKIPNI FSLQMCGAGL
     PVSGSGTNGG SLVLGGIEPS LYSGDIWYTP IKEEWYYQVE ILKLEVGGQN LQLDCREYNA
     DKAIVDSGTT LLRLPEKVFS AVVQAIARTS LIQEFSSEFW TGTQLACWDR TEKPWSLFPK
     LSIYLRDENS SRSFRISILP QLYIQPILLI GDNMQCYRFG ISSSTNALVI GATVMEGFYV
     IFDRAQRRVG FAVSPCAEVD GSPVSEIEGP FTTEDVASNC VSSVSFHEPV LWIASYALMS
     LCGIILLVLI VLLLIPPRCQ HRYTDNDVVN DESSLVRHRW K
//
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