ID A0A2T7PJY7_POMCA Unreviewed; 1908 AA.
AC A0A2T7PJY7;
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=Elongation of very long chain fatty acids protein {ECO:0000256|RuleBase:RU361115};
DE EC=2.3.1.199 {ECO:0000256|RuleBase:RU361115};
DE AltName: Full=Very-long-chain 3-oxoacyl-CoA synthase {ECO:0000256|RuleBase:RU361115};
GN ORFNames=C0Q70_04988 {ECO:0000313|EMBL:PVD33728.1};
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:PVD33728.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD33728.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD33728.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD33728.1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-
CC chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736;
CC EC=2.3.1.199; Evidence={ECO:0000256|RuleBase:RU361115};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ELO family. {ECO:0000256|RuleBase:RU361115}.
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:PVD33728.1}.
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DR EMBL; PZQS01000003; PVD33728.1; -; Genomic_DNA.
DR EnsemblMetazoa; XM_025229248.1; XP_025085033.1; LOC112558670.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009922; F:fatty acid elongase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR InterPro; IPR030457; ELO_CS.
DR InterPro; IPR002076; ELO_fam.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR11157:SF126; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN 4; 1.
DR PANTHER; PTHR11157; FATTY ACID ACYL TRANSFERASE-RELATED; 1.
DR Pfam; PF01151; ELO; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR PROSITE; PS01188; ELO; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW ECO:0000256|RuleBase:RU361115};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832,
KW ECO:0000256|RuleBase:RU361115};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|RuleBase:RU361115};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361115};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361115};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361115};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361115};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361115};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT TRANSMEM 1635..1658
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 1679..1703
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 1723..1742
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 1754..1772
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 1778..1796
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 1816..1835
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 1841..1862
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT DOMAIN 343..370
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 343..370
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1874..1908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..84
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..135
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..199
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..974
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1033
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1466..1481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1523..1573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1879..1893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1908 AA; 211965 MW; B6A0802741D86398 CRC64;
MDEGSEPLEG ELQYLSQDIS DDAMPDSQAN NKLISEIEQG DEEAEEDLNF ENAQGPEQGS
RHKSRHEHSS RHKGHKRRSH RYSRRHHEDA MEDLIEEDDE SEFPGCAGTK MTHSIEENDM
EDGEILEDGE IATDEDDDAN AKFSVPENDA ASAGDSEDHG NESESEENKT KEKSKRDRRK
KPKKEKRHKD GKQKKKSRRH AAYVDHDRLD YESGGRWSGY QGGLAEEDEN YDTHYQGSSH
YARKRHAPRD SYYYVGSSPP GLYDSPSEES DDEVPSVQQS MTSMVSDEYI DANVAANEKE
PAKVKGNAKP REKRKTRLGK RKGDIMRHIE QQPKKKPLLE IPMAERPICK FFKEGKCAKG
SSCPFNHDFK PKRLEMRHHK DFEMEPPERH IKKPSLLGSP PRHIKEAAER AKEVKKIPSL
FDIEVFPPGK EPPIPTGFYS ERSPRGEKSP PPERKSNLNS ESNQCPVGMN SPPHPGQMPM
SSQGFSPNQG PISSLGSHQP GPSLLGSPAQ GTGMVLPMRN NTQQGPMMMA GPNGPSGARP
MMGQQRPMFG MQQGMNPAMH QGMNPAMHQG MNPGMQRLQN PGMQNMNPGM QQGPRPGMQQ
GLMQVMNSNL QQGLNQVMKP GMQQGIIQNM PQNMNLNMQS MNQPINTNMQ QGMNPGMQQG
MNPGMQQGIN QSLNSNMQQG INPNMPQNMN SNMQQGINMP SIRGMNPGLQ QGMNANMQHG
MPQGIGTGML NPRIPGGPRL PFNLGGGQQT ASSMPPVLNM ISALLRGASG NGPFSQNSHQ
QQLQQAGVGV SQDTDMRRGA GGQDVHKMES PSHGNSQDSA TVEDSVSGEH EDGVCKTKQD
SDVVPESSCQ PEQKVSGQIT PLESQLEEEI AENQLSDDKE EKEEGRVTFA PDESSQQSPG
ESDSSSEDQF LSKSIGDKEN ESAIPMHLPP MQRQLFMRIR QQQLHQLQQP DVEELSEGTT
KKNTLSSHEE KHAETMDDDD DDNWYSSDEE DQDKPKAKLT DILKTITQTS GSSTVTTESH
SNSGPDSTLG TSTFSSTAST FNVMQMIQSI RNQAQTDKSV SLPTSQSSSA AGSAVTPSNT
AVSGAPSQRD PRQRQTDPRL KRSAGQEAQV MPSSGQLPLL PPLHVDPPVT NAVPHSPMTY
QISLLILPGS KVYASLPSTI DPSDPLQKAD PRVQRFLKLQ EEKAVEIKKP QDPRLRRSNS
LAEGGSSPSS RPQDPRSRRK DPRMQGMMQD PRPQPVGPQT VSGPDLHLQN VPPQEPWLQN
NMGANMMHHH MGPIGMMQQQ NNMGPGPEFQ NGMMPGPRMM QNDPRNSMMG MPGGLTNMQQ
GPMGMQQGPM GMQQRPMGMQ QGPMGMQQGP MGMQQRPMGM QQGLINMQQG PLNMQQGPMG
FGQDTRQGNL GMQQGPLGMQ QGPLAMQHDS RQNSVGMLQG PMGGLQGNMG VQHGSVGIQQ
GPIGPMGGLQ GNMGQEPHHV SVAISQDPRQ NPASNSLDSP SRAGDPRLKR GPQGDPRQVK
QPLLPVPGSG LDPRMARLGV GGQRQGLSSS PRADDSGSSP SHPTDQAYPR NSFVHSRKSS
SPSPQSSSED NFYSPEPHDL ATKKRQLLHA SPWIKSAPEE HRGSSTMEVI RDKISEFHEF
YEWAHSVSDD RVKDWLFMQG YTPTLVLSGL YLVAVYIGPK LMKDREPFKF KYTLFIYNFI
LIIMNFHICS ELFINSIALG YSYSCQPVSY TYDPREMRVA KALWWFYFSK LVEMLDTIFF
ILRKKDNQVS FLHVYHHATM FPIWYIGVKW VAGGQSFFGA MINSFIHVIM YTYYGVSALG
PEYQKYLWWK RYLTKLQLIQ FVMGITHAIQ SLVVGCDFPD WMHWALIFYA FTILMLFLNF
YFHAYIKAQK RKADNKKLTS NGKQANGYVS NGDTKLPKQW KAEAKKDK
//
