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ZDH16_BOVIN
ID   ZDH16_BOVIN             Reviewed;         377 AA.
AC   Q58CU4; Q2HJ39; Q58D89;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Palmitoyltransferase ZDHHC16 {ECO:0000250|UniProtKB:Q969W1};
DE            EC=2.3.1.225 {ECO:0000250|UniProtKB:Q969W1};
DE   AltName: Full=Zinc finger DHHC domain-containing protein 16 {ECO:0000250|UniProtKB:Q969W1};
DE            Short=DHHC-16 {ECO:0000250|UniProtKB:Q969W1};
GN   Name=ZDHHC16 {ECO:0000250|UniProtKB:Q969W1};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Palmitoyl acyltransferase that mediates palmitoylation of
CC       proteins such as PLN and ZDHHC6 (By similarity). Required during
CC       embryonic heart development and cardiac function, possibly by mediating
CC       palmitoylation of PLN, thereby affecting PLN phosphorylation and
CC       homooligomerization (By similarity). Also required for eye development
CC       (By similarity). Palmitoylates ZDHHC6, affecting the quaternary
CC       assembly of ZDHHC6, its localization, stability and function (By
CC       similarity). May play a role in DNA damage response (By similarity).
CC       May be involved in apoptosis regulation (By similarity). Involved in
CC       the proliferation of neural stem cells by regulating the FGF/ERK
CC       pathway (By similarity). {ECO:0000250|UniProtKB:B8A4F0,
CC       ECO:0000250|UniProtKB:Q969W1, ECO:0000250|UniProtKB:Q9ESG8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC         hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC         COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC         EC=2.3.1.225; Evidence={ECO:0000250|UniProtKB:Q969W1};
CC   -!- SUBUNIT: Interacts with ABL1 (By similarity). Interacts with COPS5/JAB1
CC       (By similarity). {ECO:0000250|UniProtKB:Q969W1,
CC       ECO:0000250|UniProtKB:Q9ESG8}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q969W1}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9ESG8}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q58CU4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q58CU4-2; Sequence=VSP_016273;
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000250|UniProtKB:Q8IUH5}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; BT021708; AAX46555.1; -; mRNA.
DR   EMBL; BT021853; AAX46700.1; -; mRNA.
DR   EMBL; BC113326; AAI13327.1; -; mRNA.
DR   RefSeq; NP_001019653.1; NM_001024482.2. [Q58CU4-1]
DR   RefSeq; XP_005225537.1; XM_005225480.2. [Q58CU4-1]
DR   RefSeq; XP_005225538.1; XM_005225481.2. [Q58CU4-1]
DR   RefSeq; XP_005225539.1; XM_005225482.2. [Q58CU4-1]
DR   RefSeq; XP_005225541.1; XM_005225484.2. [Q58CU4-2]
DR   RefSeq; XP_010818143.1; XM_010819841.2.
DR   AlphaFoldDB; Q58CU4; -.
DR   SMR; Q58CU4; -.
DR   STRING; 9913.ENSBTAP00000016882; -.
DR   PaxDb; Q58CU4; -.
DR   Ensembl; ENSBTAT00000016882; ENSBTAP00000016882; ENSBTAG00000012702. [Q58CU4-1]
DR   Ensembl; ENSBTAT00000016883; ENSBTAP00000016883; ENSBTAG00000012702. [Q58CU4-2]
DR   GeneID; 506085; -.
DR   KEGG; bta:506085; -.
DR   CTD; 84287; -.
DR   VEuPathDB; HostDB:ENSBTAG00000012702; -.
DR   eggNOG; KOG1313; Eukaryota.
DR   GeneTree; ENSGT00940000155032; -.
DR   HOGENOM; CLU_054274_0_0_1; -.
DR   InParanoid; Q58CU4; -.
DR   OMA; CPVRINQ; -.
DR   OrthoDB; 1491968at2759; -.
DR   TreeFam; TF320809; -.
DR   Proteomes; UP000009136; Chromosome 26.
DR   Bgee; ENSBTAG00000012702; Expressed in retina and 103 other tissues.
DR   ExpressionAtlas; Q58CU4; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016409; F:palmitoyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR   GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR   GO; GO:0018345; P:protein palmitoylation; ISS:UniProtKB.
DR   GO; GO:0021537; P:telencephalon development; ISS:UniProtKB.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   InterPro; IPR039859; ZDH16.
DR   PANTHER; PTHR12246; PTHR12246; 1.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Alternative splicing; Apoptosis; DNA damage;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..377
FT                   /note="Palmitoyltransferase ZDHHC16"
FT                   /id="PRO_0000212896"
FT   TOPO_DOM        1..79
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        101..116
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..198
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        220..266
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        288..377
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          155..205
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   ACT_SITE        185
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IUH5"
FT   VAR_SEQ         231..246
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16305752, ECO:0000303|Ref.2"
FT                   /id="VSP_016273"
SQ   SEQUENCE   377 AA;  43614 MW;  EC2FFA5D683A45E5 CRC64;
     MRGQWSLLLG PARLCLRLLL LLGYRRRCPP LLRGLVQRWR YGKVCLRSLL YNSFGGSDTA
     VDAAFEPIYW LVDNVIRWCG VVFVVLVIVL TSSIVAIAYL CVLPLILQTY SVPRLCWHFF
     YSHWNLILIV FHYYQAITTP PGYPPQGRND MTTVSICKKC INPKPARTHH CSICNRCVLK
     MDHHCPWLNN CVGHYNHRYF FSFCFFMTLG CVYCSYGSWD LFREAYAAIE KMKQLDKNKL
     QAVANQTYHQ TPPPTFSFRE RVTHKSLVYL WFLCSSVALA LGALTIWHAV LISRGETSIE
     RHINKKERQR LQAKGRVFRN HYNYGCLDNW KVFLGVDTGR HWLTRVLLPS SHLPHGNGMS
     WDPPPWVTAH SASVMAV
 
 
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