PCT2B_RAT
ID PCT2B_RAT Reviewed; 517 AA.
AC Q4V8A1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Lysophosphatidylcholine acyltransferase 2B;
DE EC=2.3.1.-;
DE AltName: Full=Acyltransferase-like 1-B;
GN Name=Lpcat2b; Synonyms=Aytl1b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Probable acetyltransferase. {ECO:0000250}.
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; BC097476; AAH97476.1; -; mRNA.
DR RefSeq; NP_001020802.1; NM_001025631.1.
DR AlphaFoldDB; Q4V8A1; -.
DR SMR; Q4V8A1; -.
DR STRING; 10116.ENSRNOP00000044422; -.
DR GlyGen; Q4V8A1; 1 site.
DR jPOST; Q4V8A1; -.
DR PaxDb; Q4V8A1; -.
DR Ensembl; ENSRNOT00000080875; ENSRNOP00000074601; ENSRNOG00000055849.
DR Ensembl; ENSRNOT00000096698; ENSRNOP00000089831; ENSRNOG00000055849.
DR GeneID; 289439; -.
DR KEGG; rno:289439; -.
DR UCSC; RGD:1310837; rat.
DR CTD; 70902; -.
DR RGD; 1310837; Lpcat2b.
DR eggNOG; KOG4666; Eukaryota.
DR GeneTree; ENSGT01030000234574; -.
DR HOGENOM; CLU_025017_0_0_1; -.
DR InParanoid; Q4V8A1; -.
DR OMA; HISAWRW; -.
DR OrthoDB; 1266853at2759; -.
DR PhylomeDB; Q4V8A1; -.
DR UniPathway; UPA00085; -.
DR PRO; PR:Q4V8A1; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000055849; Expressed in testis and 3 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
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; PF00036; EF-hand_1; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 2: Evidence at transcript level;
KW Acyltransferase; Calcium; Glycoprotein; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Metal-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Repeat; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..517
FT /note="Lysophosphatidylcholine acyltransferase 2B"
FT /id="PRO_0000247062"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 388..423
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 425..460
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOTIF 143..148
FT /note="HXXXXD motif"
FT BINDING 401
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 438
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 440
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 442
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 449
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 517 AA; 58563 MW; B88ABC18AEF2C34C CRC64;
MAHQTQRRDT ADTMTEVEVW DSRTAQEVNK SLYPPAVTNP FTHHTQLSAW QLACSIFLGT
VLVPVRVSCI VFLFLLLWPV ALLSTINLPI QPTEPVKSWR KHLIKPVFIF LLRLAFFCAG
FLIKVKGKKA TREEAPIFVV APHSTFFDAI AVIVAGLPSV VSDTQHVRIP LVGQCILLTQ
PVLVRREDPN SRKTTRNEIL SRVKSKMKWP QILIFPEGLC TNRSCLVTFK LGAFSPGVPV
QPVLLRYPNT LDTVTWTWHG FSGFQVCMLT LSQPFTRMEV EFMPVYIPNE DEKKDPILFA
NTVRINMANA LKLPVTDHSF EDCKLMISAG ALRLPMEAGL VEFTKISQKL KLDWDNIHTH
LDKYASVAVS SKGGKIGIEE FSRYLKLPIS EPLRQLFSLF DRNQDGTIDF REYVIGLTVL
CNPANTEKIL QMSFKLFDLD EDGYITEQEL TTMLRAAFGV PDLDVSTLFQ QMAGKDSAQV
SYRTFRRFAL KHPAYAKLFH SYIDLQAAYI YSLPGEV
