ID A0A493T0C5_ANAPP Unreviewed; 1201 AA.
AC A0A493T0C5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=N-acetylglucosamine-1-phosphate transferase subunits alpha and beta {ECO:0000313|Ensembl:ENSAPLP00000019155.1};
GN Name=GNPTAB {ECO:0000313|Ensembl:ENSAPLP00000019155.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000019155.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000019155.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000019155.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 stealth family.
CC {ECO:0000256|ARBA:ARBA00007583}.
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DR AlphaFoldDB; A0A493T0C5; -.
DR Ensembl; ENSAPLT00000018690.1; ENSAPLP00000019155.1; ENSAPLG00000016228.2.
DR GeneTree; ENSGT00390000006747; -.
DR Proteomes; UP000016666; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
DR CDD; cd21599; RRM1_GNPTAB; 1.
DR CDD; cd21600; RRM2_GNPTAB; 1.
DR Gene3D; 3.30.300.320; -; 1.
DR InterPro; IPR010506; DMAP1-bd.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR041536; GNPTAB_reg.
DR InterPro; IPR035993; Notch-like_dom_sf.
DR InterPro; IPR000800; Notch_dom.
DR InterPro; IPR047141; Stealth.
DR InterPro; IPR021520; Stealth_CR2.
DR InterPro; IPR031357; Stealth_CR3.
DR InterPro; IPR031356; Stealth_CR4.
DR PANTHER; PTHR24045; -; 1.
DR PANTHER; PTHR24045:SF0; N-ACETYLGLUCOSAMINE-1-PHOSPHOTRANSFERASE SUBUNITS ALPHA_BETA; 1.
DR Pfam; PF06464; DMAP_binding; 1.
DR Pfam; PF18440; GlcNAc-1_reg; 1.
DR Pfam; PF00066; Notch; 2.
DR Pfam; PF11380; Stealth_CR2; 1.
DR Pfam; PF17102; Stealth_CR3; 1.
DR Pfam; PF17103; Stealth_CR4; 1.
DR SMART; SM01137; DMAP_binding; 1.
DR SMART; SM00004; NL; 2.
DR SUPFAM; SSF90193; Notch domain; 1.
DR PROSITE; PS51912; DMAP1_BIND; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50258; LNR; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1155..1180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 375..410
FT /note="LNR"
FT /evidence="ECO:0000259|PROSITE:PS50258"
FT DOMAIN 636..750
FT /note="DMAP1-binding"
FT /evidence="ECO:0000259|PROSITE:PS51912"
FT DOMAIN 950..985
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 746..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1201 AA; 136882 MW; 9B6BB7A2BBB918B8 CRC64;
MVLLFLLVCV GALGIILLSL IFLHHHCSTC ALIFISFCMH KADTREILGK NATEPTKKSE
KQLECLLTHC IKVPMLVLDP ALPTNVTLKD LLSIHPALQA ANNMFFVAKP KNPSTNVTVI
VFDSPKDVEA AHSGMLKDNS KQIVWRGYLT TDKEVPGLVL MQDLAFLSGF PATFKETNQL
RTKLPESLAS KVKLLQLYSE ASVALLQLNN PKGFHELSKQ AKKNMTIDGK ELTLNPAYLL
WDLSSVSQSK QDEDISASRF EDNEELRYSL RSIERHAPWV RHIFIVTNGQ IPSWLNLDNP
RITIVTHQEI FQNVSHLPTF SSPAIESHIH RISGLSQKFI YLNDDVMFGK DVWPDDFYSH
SKGQKVYLTW PVPNCAEGCP GSWIKDGYCD KACNNSACDW DGGDCIGNSG GSRYVAGGGA
VGGIGNGPPW QFGGGISGVS YCNQGCANSW LADKFCDQAC NVLSCGFDAG DCGQDHFEEM
YKVTLQLNQT YYVIPKGECL LYFSFSEIAK KGIEGSYSDN PIIRHASVAN KWKTIHLIMH
SGMNTTVIYF NLTFLNKNDE EFKMQVAIEV DTREEPKLNA SSTQKSNSDF KTPTSIPEAE
MIFEDIPEEK RFPRVRRRRN ETGGSFHEEI IIPSVNESLL PENVKIALQN LDLKLENGDI
TQKGFNLSKA ALLRPYQFST TVKKIVGLEK NDVHYNSQDK KNETIWQKPH EDVNNSKTET
AIKANGEVPS RLTRTKRTDV AMNTNKPISK MKPKSTQPAQ RNGIQSMGNE NEPQEKVLNS
LILRETQKSK NIRNSEAGED TEGMEGRKGH EQLDTNVREG LVGRKLQSYA GSYQGFLPWE
KKKYFQDLLD EEESLLKEMS YFTDGKHLGR QLKDTFADSL RYVNKLLNSK FGFTSRKVPA
HMPHMIDRTV MQELQDMFPE EFDKTSFHKV RHSEDMQFAF SYFYYLMSAV QPLNISQIFD
EVDTDQSGIL SDREIRTLAT RIHELPLSLQ DLTGLEQMLI NCSKSLPANI TRIHVIPPTQ
EAYYDPNLPP VTKNLVTNCK PVTDRIRKAY KDKNKYRFEI MGEEEIAFKM IRTNVSHVVG
QLDDIRKNPR KFVCLNDNID HNHKDAQTVK AVLRDFYESM FPIPSQFELP REYRNRFLHM
HELQEWRAYR DKLKFWTHCV LVTLIVFTVI SFFAEQLIAL KRKIFPRRRI QKEDGHERIK
V
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