FABP1_DORPE
ID FABP1_DORPE Reviewed; 132 AA.
AC C4N147;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Sodium/calcium exchanger regulatory protein 1 {ECO:0000303|PubMed:19168028};
DE Short=ReP1-NCXSQ {ECO:0000303|PubMed:19168028};
DE AltName: Full=Fatty acid-binding protein 1 {ECO:0000305};
DE AltName: Full=Na(+)/Ca(2+) exchanger regulatory protein 1 {ECO:0000303|PubMed:19168028};
OS Doryteuthis pealeii (Longfin inshore squid) (Loligo pealeii).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Decapodiformes; Teuthida; Myopsina; Loliginidae; Doryteuthis.
OX NCBI_TaxID=1051067 {ECO:0000312|EMBL:ACL80558.1};
RN [1] {ECO:0000312|EMBL:ACL80558.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND PHOSPHORYLATION.
RC TISSUE=Cervicothoracic ganglion {ECO:0000312|EMBL:ACL80558.1};
RX PubMed=19168028; DOI=10.1016/j.bbamem.2008.12.016;
RA Berberian G., Bollo M., Montich G., Roberts G., Degiorgis J.A., Dipolo R.,
RA Beauge L.;
RT "A novel lipid binding protein is a factor required for MgATP stimulation
RT of the squid nerve Na+/Ca2+ exchanger.";
RL Biochim. Biophys. Acta 1788:1255-1262(2009).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH NCXSQ1, AND PHOSPHORYLATION.
RX PubMed=19386360; DOI=10.1016/j.ceca.2009.03.009;
RA Raimunda D., Bollo M., Beauge L., Berberian G.;
RT "Squid nerve Na+/Ca2+ exchanger expressed in Saccharomyces cerevisiae: up-
RT regulation by a phosphorylated cytosolic protein (ReP1-NCXSQ) is identical
RT to that of native exchanger in situ.";
RL Cell Calcium 45:499-508(2009).
RN [3] {ECO:0000305}
RP FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF TYR-20; PHE-58; SER-99;
RP ARG-126 AND TYR-128.
RX PubMed=23224877; DOI=10.1007/978-1-4614-4756-6_13;
RA Beauge L., Dipolo R., Bollo M., Cousido A., Berberian G., Podjarny A.;
RT "Metabolic regulation of the squid nerve Na(+)/Ca (2+) exchanger: recent
RT developments.";
RL Adv. Exp. Med. Biol. 961:149-161(2013).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=24269200; DOI=10.1016/j.bbamem.2013.11.008;
RA Galassi V.V., Villarreal M.A., Posada V., Montich G.G.;
RT "Interactions of the fatty acid-binding protein ReP1-NCXSQ with lipid
RT membranes. Influence of the membrane electric field on binding and
RT orientation.";
RL Biochim. Biophys. Acta 1838:910-920(2014).
RN [5] {ECO:0007744|PDB:3PP6, ECO:0007744|PDB:3PPT}
RP X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) OF 2-132 IN COMPLEX WITH PALMITOLEIC
RP ACID, FUNCTION, DOMAIN, AND MUTAGENESIS OF TYR-128.
RX PubMed=22948910; DOI=10.1107/s090744491202094x;
RA Cousido-Siah A., Ayoub D., Berberian G., Bollo M., Van Dorsselaer A.,
RA Debaene F., DiPolo R., Petrova T., Schulze-Briese C., Olieric V.,
RA Esteves A., Mitschler A., Sanglier-Cianferani S., Beauge L., Podjarny A.;
RT "Structural and functional studies of ReP1-NCXSQ, a protein regulating the
RT squid nerve Na+/Ca2+ exchanger.";
RL Acta Crystallogr. D 68:1098-1107(2012).
CC -!- FUNCTION: Binds and may transport fatty acids such as palmitoleate
CC (PubMed:22948910). Also binds poly-phosphoinositides including
CC phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol
CC 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol 3,4,5-
CC trisphosphate (PtdIns(3,4,5)P3), and phosphatidic acid
CC (PubMed:19168028). When phosphorylated, stimulates the activity of
CC optic nerve Na(+)/Ca(2+) exchanger (PubMed:19168028, PubMed:19386360,
CC PubMed:22948910). {ECO:0000269|PubMed:19168028,
CC ECO:0000269|PubMed:19386360, ECO:0000269|PubMed:22948910}.
CC -!- SUBUNIT: Interacts with Na(+)/Ca(2+) exchanger NCXSQ1; ReP1-NCXSQ
CC phosphorylation does not affect the interaction.
CC {ECO:0000269|PubMed:19386360}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19168028}. Membrane
CC {ECO:0000269|PubMed:24269200}; Peripheral membrane protein
CC {ECO:0000269|PubMed:24269200}.
CC -!- TISSUE SPECIFICITY: Expressed in the optic nerve (at protein level).
CC {ECO:0000269|PubMed:19168028}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior. {ECO:0000269|PubMed:22948910}.
CC -!- PTM: Phosphorylated (PubMed:19168028, PubMed:23224877,
CC PubMed:19386360). Phosphorylation may result in the release of the
CC bound fatty acid (PubMed:22948910). {ECO:0000269|PubMed:19168028,
CC ECO:0000269|PubMed:19386360, ECO:0000269|PubMed:22948910,
CC ECO:0000269|PubMed:23224877}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000255, ECO:0000255|RuleBase:RU003696}.
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; EU981897; ACL80558.1; -; mRNA.
DR PDB; 3PP6; X-ray; 1.90 A; A/B/C=2-132.
DR PDB; 3PPT; X-ray; 1.28 A; A=2-132.
DR PDBsum; 3PP6; -.
DR PDBsum; 3PPT; -.
DR AlphaFoldDB; C4N147; -.
DR SMR; C4N147; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00214; FABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipid-binding; Membrane; Phosphoprotein;
KW Transport.
FT CHAIN 1..132
FT /note="Sodium/calcium exchanger regulatory protein 1"
FT /id="PRO_0000445547"
FT BINDING 126
FT /ligand="(9Z)-hexadecenoate"
FT /ligand_id="ChEBI:CHEBI:32372"
FT /evidence="ECO:0000269|PubMed:22948910,
FT ECO:0007744|PDB:3PPT"
FT BINDING 128
FT /ligand="(9Z)-hexadecenoate"
FT /ligand_id="ChEBI:CHEBI:32372"
FT /evidence="ECO:0000269|PubMed:22948910,
FT ECO:0007744|PDB:3PPT"
FT MUTAGEN 20
FT /note="Y->F: Does not affect activation of Na(+)/Ca(2+)
FT exchanger and ReP1-NCXSQ phosphorylation."
FT /evidence="ECO:0000269|PubMed:23224877"
FT MUTAGEN 58
FT /note="F->V: Does not affect activation of Na(+)/Ca(2+)
FT exchanger and ReP1-NCXSQ phosphorylation."
FT /evidence="ECO:0000269|PubMed:23224877"
FT MUTAGEN 99
FT /note="S->A: Does not affect activation of Na(+)/Ca(2+)
FT exchanger and ReP1-NCXSQ phosphorylation."
FT /evidence="ECO:0000269|PubMed:23224877"
FT MUTAGEN 126
FT /note="R->A: Does not affect activation of Na(+)/Ca(2+)
FT exchanger and ReP1-NCXSQ phosphorylation. Fails to activate
FT Na(+)/Ca(2+) exchanger and does not affect ReP1-NCXSQ
FT phosphorylation; when associated with F-128."
FT /evidence="ECO:0000269|PubMed:23224877"
FT MUTAGEN 128
FT /note="Y->F: Loss of binding to fatty acid. Fails to
FT activate Na(+)/Ca(2+) exchanger. Does not affect ReP1-NCXSQ
FT phosphorylation. Fails to activate Na(+)/Ca(2+) exchanger
FT and does not affect ReP1-NCXSQ phosphorylation; when
FT associated with A-126."
FT /evidence="ECO:0000269|PubMed:22948910,
FT ECO:0000269|PubMed:23224877"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:3PPT"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:3PPT"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:3PPT"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:3PPT"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:3PPT"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:3PPT"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:3PPT"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:3PPT"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:3PPT"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:3PPT"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:3PPT"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:3PPT"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:3PPT"
SQ SEQUENCE 132 AA; 14664 MW; AD7446861972E746 CRC64;
MAADLAGKWI LESSENFDDY MKAVGVGMVM RKMANAATPT QEIKIDGDSW SIKTSTTFKT
TDISFTIGQE FDETTGDGRK IKTTCKIDGN AMIQDQKGSP DSILSREVKD GKMHMILKVN
DVVCTRIYKR VD
