PCAT2_DANRE
ID PCAT2_DANRE Reviewed; 529 AA.
AC Q502J0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Lysophosphatidylcholine acyltransferase 2;
DE Short=LPC acyltransferase 2;
DE Short=LPCAT-2;
DE Short=LysoPC acyltransferase 2;
DE EC=2.3.1.23 {ECO:0000250|UniProtKB:Q7L5N7};
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 11;
DE Short=1-AGP acyltransferase 11;
DE Short=1-AGPAT 11;
DE EC=2.3.1.51 {ECO:0000250|UniProtKB:Q7L5N7};
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE AltName: Full=1-alkenylglycerophosphocholine O-acyltransferase;
DE EC=2.3.1.25 {ECO:0000250|UniProtKB:Q8BYI6};
DE AltName: Full=1-alkylglycerophosphocholine O-acetyltransferase;
DE EC=2.3.1.67 {ECO:0000250|UniProtKB:Q8BYI6};
DE AltName: Full=Acyltransferase-like 1;
GN Name=lpcat2; Synonyms=aytl1; ORFNames=zgc:112165;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Larva;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Exhibits both acyltransferase and acetyltransferase
CC activities (By similarity). Activity is calcium-dependent (By
CC similarity). Catalyzes the conversion of lysophosphatidylcholine (1-
CC acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-
CC diacyl-sn-glycero-3-phosphocholine or PC) (By similarity). Catalyzes
CC the conversion 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or
CC LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA)
CC by incorporating an acyl moiety at the sn-2 position of the glycerol
CC backbone (By similarity). Involved in platelet-activating factor (PAF)
CC biosynthesis by catalyzing the conversion of the PAF precursor, 1-O-
CC alkyl-sn-glycero-3-phosphocholine (lyso-PAF) into 1-O-alkyl-2-acetyl-
CC sn-glycero-3-phosphocholine (PAF) (By similarity).
CC {ECO:0000250|UniProtKB:Q7L5N7, ECO:0000250|UniProtKB:Q8BYI6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:58342; EC=2.3.1.23;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-alkyl-sn-glycero-3-phosphocholine + acetyl-CoA = a 1-O-
CC alkyl-2-acetyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:18461, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.67;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + an acyl-CoA =
CC 1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:10344, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:77286, ChEBI:CHEBI:77287; EC=2.3.1.25;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate
CC = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:33187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:64839;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74546;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37143, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74551;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-heptadecanoyl-sn-glycero-3-phosphate
CC = 1-heptadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37151, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74554, ChEBI:CHEBI:74556;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37152;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phosphate
CC = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37163, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74560, ChEBI:CHEBI:74565;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37164;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + heptadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-heptadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37155, ChEBI:CHEBI:57287, ChEBI:CHEBI:74307,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74558;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37156;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphate = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-
CC glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37159, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:74544, ChEBI:CHEBI:74563;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37160;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + tetradecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-tetradecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37171, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74579;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37172;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + pentadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-pentadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37175, ChEBI:CHEBI:57287, ChEBI:CHEBI:74309,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74578;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37176;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + nonadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-nonadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37595, ChEBI:CHEBI:57287, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:75104, ChEBI:CHEBI:75105;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37596;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:35991, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-sn-glycero-3-phosphocholine + acetyl-CoA = 1-O-
CC hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37719, ChEBI:CHEBI:44811, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:64496;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37720;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-octadecyl-sn-glycero-3-phosphocholine + acetyl-CoA = 1-O-
CC octadecyl-2-acetyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37699, ChEBI:CHEBI:52450, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:75216;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37700;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + acetyl-CoA = 1-
CC hexadecanoyl-2-acetyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37703, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:75219;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37704;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-sn-glycero-3-phosphocholine + acetyl-CoA = 1-
CC octadecanoyl-2-acetyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37707, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:73858, ChEBI:CHEBI:75220;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37708;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + acetyl-CoA = 1-
CC O-(1Z)-alkenyl-2-acetyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37711, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:77287, ChEBI:CHEBI:78566;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37712;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-O-octadecyl-sn-
CC glycero-3-phosphocholine = 1-O-octadecyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37747, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:75216, ChEBI:CHEBI:75245;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37748;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q7L5N7}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q7L5N7}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8BYI6}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q7L5N7}. Cell membrane
CC {ECO:0000250|UniProtKB:Q8BYI6}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q7L5N7}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q7L5N7}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity.
CC {ECO:0000250|UniProtKB:Q3TFD2}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; BC095679; AAH95679.1; -; mRNA.
DR RefSeq; NP_001018492.1; NM_001020656.1.
DR AlphaFoldDB; Q502J0; -.
DR SMR; Q502J0; -.
DR STRING; 7955.ENSDARP00000069449; -.
DR PaxDb; Q502J0; -.
DR GeneID; 553683; -.
DR KEGG; dre:553683; -.
DR CTD; 54947; -.
DR ZFIN; ZDB-GENE-050522-229; lpcat2.
DR eggNOG; KOG4666; Eukaryota.
DR InParanoid; Q502J0; -.
DR PhylomeDB; Q502J0; -.
DR Reactome; R-DRE-1482788; Acyl chain remodelling of PC.
DR UniPathway; UPA00085; -.
DR PRO; PR:Q502J0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047159; F:1-alkenylglycerophosphocholine O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047192; F:1-alkylglycerophosphocholine O-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050200; F:plasmalogen synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 2.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 3.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 2: Evidence at transcript level;
KW Acyltransferase; Calcium; Cell membrane; Endoplasmic reticulum;
KW Glycoprotein; Golgi apparatus; Lipid biosynthesis; Lipid droplet;
KW Lipid metabolism; Membrane; Metal-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Repeat; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..529
FT /note="Lysophosphatidylcholine acyltransferase 2"
FT /id="PRO_0000247063"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..529
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 373..408
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 410..445
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 449..480
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOTIF 128..133
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q3TFD2"
FT MOTIF 202..205
FT /note="EGTC motif"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 397
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 423
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 425
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 427
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 429
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 434
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 458
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 460
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 462
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 464
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 529 AA; 59424 MW; F54CA365FE6461D1 CRC64;
MPPPHRVFAL PRQQSLLLPA VINPFVHDLS LSTADITKCF LLGIILVPLR AIFLLLVLLV
MWPVSVIITF GQSLKGVVEP MTGWRRFLHR RVMTFLGRMY FFGMGFKVVV KGKKASTLEA
PILAVAPHSS FFDAIACIES GLPSTVSRIE SLEAPIFGRF LRCVQPVLVS RTDPDSRRNT
IIEIERRAKS GGHWPQVLIF PEGTCTNRSC LITFKQGGFV PGVPVQPVLI RYPNKLDTVT
WTWQGPKSAR LLLLTLCQLC TTVEVEFLPP QVPTEMEKKC PLKFAQSVRA VMAKSLKLPV
TDHTYEDCRL MIAAGELTLP MEAGLVEFTK ISRKLELKWD NVKKELESFA NIACSCKGGR
ITVEEFASFL KLPISPALQQ LFALFDRNGD GTIDFREYVI GVTVLCRPAN NEEVIQTAFK
LFDIDEDNCI TQEEFSSLLR SALGVCDLDV HSLFREIDAD GSGHITYDEF RSFALNHPEY
AKLFTTYIEL QRYQGLQGDE TDFDSAFSHC CTAAYDEYQE DSASDKKDD
