CABP7_HUMAN
ID CABP7_HUMAN Reviewed; 215 AA.
AC Q86V35;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Calcium-binding protein 7;
DE Short=CaBP7;
DE AltName: Full=Calneuron II;
DE AltName: Full=Calneuron-2;
GN Name=CABP7; Synonyms=CALN2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=19338761; DOI=10.1016/j.bbrc.2009.01.177;
RA McCue H.V., Burgoyne R.D., Haynes L.P.;
RT "Membrane targeting of the EF-hand containing calcium-sensing proteins
RT CaBP7 and CaBP8.";
RL Biochem. Biophys. Res. Commun. 380:825-831(2009).
RN [3]
RP STRUCTURE BY NMR OF 1-100, AND CALCIUM-BINDING SITES.
RX PubMed=22989873; DOI=10.1074/jbc.m112.402289;
RA McCue H.V., Patel P., Herbert A.P., Lian L.Y., Burgoyne R.D., Haynes L.P.;
RT "Solution NMR structure of the Ca2+-bound N-terminal domain of CaBP7: a
RT regulator of golgi trafficking.";
RL J. Biol. Chem. 287:38231-38243(2012).
CC -!- FUNCTION: Negatively regulates Golgi-to-plasma membrane trafficking by
CC interacting with PI4KB and inhibiting its activity. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PI4KB. This binding competes with FREQ/NCS1
CC binding in a calcium-dependent manner (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q86V35; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-23900553, EBI-3923617;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000305|PubMed:19338761}; Single-pass type IV membrane protein
CC {ECO:0000305|PubMed:19338761}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:19338761}. Cell membrane
CC {ECO:0000305|PubMed:19338761}; Single-pass type IV membrane protein
CC {ECO:0000305|PubMed:19338761}.
CC -!- DOMAIN: The C-terminal transmembrane domain (TMD) is necessary and
CC sufficient for membrane targeting.
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DR EMBL; BC051805; AAH51805.1; -; mRNA.
DR CCDS; CCDS13867.1; -.
DR RefSeq; NP_872333.1; NM_182527.2.
DR PDB; 2LV7; NMR; -; A=1-100.
DR PDBsum; 2LV7; -.
DR AlphaFoldDB; Q86V35; -.
DR BMRB; Q86V35; -.
DR SMR; Q86V35; -.
DR BioGRID; 127897; 2.
DR IntAct; Q86V35; 1.
DR STRING; 9606.ENSP00000216144; -.
DR iPTMnet; Q86V35; -.
DR PhosphoSitePlus; Q86V35; -.
DR BioMuta; CABP7; -.
DR DMDM; 37537777; -.
DR jPOST; Q86V35; -.
DR MaxQB; Q86V35; -.
DR PaxDb; Q86V35; -.
DR PeptideAtlas; Q86V35; -.
DR PRIDE; Q86V35; -.
DR ProteomicsDB; 69960; -.
DR Antibodypedia; 24571; 115 antibodies from 28 providers.
DR DNASU; 164633; -.
DR Ensembl; ENST00000216144.4; ENSP00000216144.3; ENSG00000100314.4.
DR GeneID; 164633; -.
DR KEGG; hsa:164633; -.
DR MANE-Select; ENST00000216144.4; ENSP00000216144.3; NM_182527.3; NP_872333.1.
DR UCSC; uc003agl.4; human.
DR CTD; 164633; -.
DR GeneCards; CABP7; -.
DR HGNC; HGNC:20834; CABP7.
DR HPA; ENSG00000100314; Tissue enriched (brain).
DR MIM; 618759; gene.
DR neXtProt; NX_Q86V35; -.
DR OpenTargets; ENSG00000100314; -.
DR PharmGKB; PA134928335; -.
DR VEuPathDB; HostDB:ENSG00000100314; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000159368; -.
DR HOGENOM; CLU_106115_0_0_1; -.
DR InParanoid; Q86V35; -.
DR OMA; CPVEVET; -.
DR OrthoDB; 1542616at2759; -.
DR PhylomeDB; Q86V35; -.
DR TreeFam; TF331025; -.
DR PathwayCommons; Q86V35; -.
DR SignaLink; Q86V35; -.
DR BioGRID-ORCS; 164633; 11 hits in 1062 CRISPR screens.
DR ChiTaRS; CABP7; human.
DR GenomeRNAi; 164633; -.
DR Pharos; Q86V35; Tbio.
DR PRO; PR:Q86V35; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q86V35; protein.
DR Bgee; ENSG00000100314; Expressed in pons and 96 other tissues.
DR Genevisible; Q86V35; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Cytoplasm; Golgi apparatus; Membrane;
KW Metal-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..215
FT /note="Calcium-binding protein 7"
FT /id="PRO_0000073526"
FT TOPO_DOM 1..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 33..68
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 69..104
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2LV7"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:2LV7"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:2LV7"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:2LV7"
FT HELIX 55..64
FT /evidence="ECO:0007829|PDB:2LV7"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:2LV7"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:2LV7"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:2LV7"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:2LV7"
SQ SEQUENCE 215 AA; 24453 MW; 9C254C955F7AFFA8 CRC64;
MPFHPVTAAL MYRGIYTVPN LLSEQRPVDI PEDELEEIRE AFKVFDRDGN GFISKQELGT
AMRSLGYMPN EVELEVIIQR LDMDGDGQVD FEEFVTLLGP KLSTSGIPEK FHGTDFDTVF
WKCDMQKLTV DELKRLLYDT FCEHLSMKDI ENIIMTEEES HLGTAEECPV DVETCSNQQI
RQTCVRKSLI CAFAIAFIIS VMLIAANQVL RSGMK
