GenomeNet

Database: UniProt
Entry: A0A2T7P375_POMCA
LinkDB: A0A2T7P375_POMCA
Original site: A0A2T7P375_POMCA 
ID   A0A2T7P375_POMCA        Unreviewed;       764 AA.
AC   A0A2T7P375;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Dystrophin {ECO:0008006|Google:ProtNLM};
GN   ORFNames=C0Q70_10444 {ECO:0000313|EMBL:PVD27869.1};
OS   Pomacea canaliculata (Golden apple snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX   NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD27869.1, ECO:0000313|Proteomes:UP000245119};
RN   [1] {ECO:0000313|EMBL:PVD27869.1, ECO:0000313|Proteomes:UP000245119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD27869.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PVD27869.1};
RA   Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA   Zhang G., Qian W., Fan W.;
RT   "The genome of golden apple snail Pomacea canaliculata provides insight
RT   into stress tolerance and invasive adaptation.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PVD27869.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; PZQS01000006; PVD27869.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7P375; -.
DR   STRING; 400727.A0A2T7P375; -.
DR   EnsemblMetazoa; XM_025243519.1; XP_025099304.1; LOC112567040.
DR   Proteomes; UP000245119; Miscellaneous, Linkage group lg6.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   CDD; cd14686; bZIP; 1.
DR   CDD; cd16242; EFh_DMD_like; 1.
DR   CDD; cd00176; SPEC; 1.
DR   CDD; cd00201; WW; 1.
DR   CDD; cd02334; ZZ_dystrophin; 1.
DR   Gene3D; 1.20.58.60; -; 1.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 3.30.60.90; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR015153; EF-hand_dom_typ1.
DR   InterPro; IPR015154; EF-hand_dom_typ2.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   InterPro; IPR000433; Znf_ZZ.
DR   InterPro; IPR043145; Znf_ZZ_sf.
DR   PANTHER; PTHR12268:SF14; DYSTROPHIN-1; 1.
DR   PANTHER; PTHR12268; E3 UBIQUITIN-PROTEIN LIGASE KCMF1; 1.
DR   Pfam; PF09068; EF-hand_2; 1.
DR   Pfam; PF09069; EF-hand_3; 1.
DR   Pfam; PF00435; Spectrin; 1.
DR   Pfam; PF00397; WW; 1.
DR   Pfam; PF00569; ZZ; 1.
DR   SMART; SM00150; SPEC; 1.
DR   SMART; SM00456; WW; 1.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF47473; EF-hand; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 1.
DR   SUPFAM; SSF51045; WW domain; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00228}.
FT   DOMAIN          120..153
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          377..433
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   REGION          573..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          653..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..28
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          618..652
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        573..590
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..680
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   764 AA;  85706 MW;  B011B19875545177 CRC64;
     MTLFHEAMED LEQHLTEAER EKGAWQGVGD ILIKELPAEI EATKNFQQKY APLQGEIDSV
     NDQANDLQSA DVILSHVNVR RLEDFNTRWK ALQISIEDRL KQLQDALRAF GPHSQHFLAA
     SVASPWERAV AGNKVPYFIN HVTEKTQWDH PVFAVLFDEL SALNDIRFAA YRTGMKLRML
     QKKLGLHLVD MTVASEAFER HGLRGQNDKL IEVTEMIECL SSMYEQIAAQ RSTSSVPVDV
     PLCVDLVLNW ILNVYDTVRS GKVRVLSFKV GVILLCSGQL EDKYRFMFRL IADTNGFADQ
     RKLGLLLHDC IQIPLQLGEV AAFGGSNIEP SVRSCFEKAK GRPEIQVGHF LDWLSLEPQS
     LVWLPVLHRL AAAETAKHQA KCNVCKDFPI IGFRYRCLKC FNFDMCQNCF FSGRLVKGHK
     LSHPMQEYCT TTTSGEDVRD FSKVFKNKFK SKRHFKKHPR LGYLPVQTVL EGDSLESPAP
     SPQHSILMSQ DMHSRLELYA SRLAEVEQRQ NCSSPDSEDE HHLIAQYCSS LNGDPSAQAL
     KSPMQIMLAV DAEQQQELEA TIKELEQENR TLQEEYNRLR EARESRESST LSEDGGNISG
     NIRDEEMLAE AKLLRQHKGR LEARMRILED HNHQLEAQLA RLRQLLDQSQ GDRSLASINS
     SSRSTPITTP SSSQSSLPGG LGRYRFTPTA ESSQHLNGHS SGIVGTEETS ITAGDNTASS
     ITTDKSKGNV GELFHIAGEV GQAVGSLVTV MTDQEGGVVE ESRH
//
DBGET integrated database retrieval system