NUCB1_BOVIN
ID NUCB1_BOVIN Reviewed; 474 AA.
AC Q0P569;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Nucleobindin-1;
DE Flags: Precursor;
GN Name=NUCB1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 25-32; 111-115 AND 411-418, FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=7890746; DOI=10.1074/jbc.270.11.6125;
RA Wendel M., Sommarin Y., Bergman T., Heinegaard D.;
RT "Isolation, characterization, and primary structure of a calcium-binding
RT 63-kDa bone protein.";
RL J. Biol. Chem. 270:6125-6133(1995).
CC -!- FUNCTION: Major calcium-binding protein of the Golgi which may have a
CC role in calcium homeostasis (PubMed:7890746). Acts as a non-receptor
CC guanine nucleotide exchange factor which binds to and activates alpha
CC subunits of guanine nucleotide-binding proteins (G proteins) (By
CC similarity). {ECO:0000250|UniProtKB:Q63083,
CC ECO:0000269|PubMed:7890746}.
CC -!- SUBUNIT: Interacts (via GBA motif) with guanine nucleotide-binding
CC protein G(i) alpha subunits GNAI1, GNAI2 and GNAI3 with higher affinity
CC for GNAI1 and GNAI3 than for GNAI2. Preferentially interacts with
CC inactive rather than active GNAI3. Interaction with GNAI3 is inhibited
CC when NUCB1 binds calcium, probably due to a conformational change which
CC renders the GBA motif inaccessible. {ECO:0000250|UniProtKB:Q63083}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q63083}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q63083}; Lumenal side
CC {ECO:0000250|UniProtKB:Q63083}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q63083}. Secreted
CC {ECO:0000250|UniProtKB:Q63083}. Note=A small fraction of the protein
CC may be cytoplasmic. {ECO:0000250|UniProtKB:Q63083}.
CC -!- TISSUE SPECIFICITY: Expressed in bone where it is detected in the soft
CC tissue in the center of the osteon and in the osteocyte lacuna (at
CC protein level). {ECO:0000269|PubMed:7890746}.
CC -!- DOMAIN: The EF-hand domains are unfolded in the absence of Ca(2+) and
CC fold upon Ca(2+) addition. {ECO:0000250|UniProtKB:Q02818}.
CC -!- DOMAIN: The GBA (G-alpha binding and activating) motif mediates binding
CC to the alpha subunits of guanine nucleotide-binding proteins (G
CC proteins). {ECO:0000250|UniProtKB:Q63083}.
CC -!- SIMILARITY: Belongs to the nucleobindin family. {ECO:0000305}.
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DR EMBL; BC120433; AAI20434.1; -; mRNA.
DR RefSeq; NP_001068667.1; NM_001075199.1.
DR RefSeq; XP_010813309.1; XM_010815007.1.
DR AlphaFoldDB; Q0P569; -.
DR BMRB; Q0P569; -.
DR SMR; Q0P569; -.
DR STRING; 9913.ENSBTAP00000003073; -.
DR PaxDb; Q0P569; -.
DR PeptideAtlas; Q0P569; -.
DR PRIDE; Q0P569; -.
DR GeneID; 505351; -.
DR KEGG; bta:505351; -.
DR CTD; 4924; -.
DR eggNOG; KOG3866; Eukaryota.
DR HOGENOM; CLU_031153_1_0_1; -.
DR InParanoid; Q0P569; -.
DR OrthoDB; 1339224at2759; -.
DR TreeFam; TF323218; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISS:UniProtKB.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR040253; NUCB1.
DR InterPro; IPR040250; Nucleobindin.
DR PANTHER; PTHR19237; PTHR19237; 1.
DR PANTHER; PTHR19237:SF21; PTHR19237:SF21; 1.
DR Pfam; PF13499; EF-hand_7; 1.
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 Calcium; Coiled coil; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Golgi apparatus; Guanine-nucleotide releasing factor; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:7890746"
FT CHAIN 25..474
FT /note="Nucleobindin-1"
FT /id="PRO_0000287127"
FT DOMAIN 237..272
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 289..324
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 190..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..318
FT /note="Binds to GNAI2 and GNAI3"
FT /evidence="ECO:0000250"
FT REGION 382..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 147..215
FT /evidence="ECO:0000255"
FT COILED 355..422
FT /evidence="ECO:0000255"
FT MOTIF 300..330
FT /note="GBA"
FT /evidence="ECO:0000250|UniProtKB:Q02818"
FT COMPBIAS 190..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 302
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 313
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02818"
FT MOD_RES 145
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q02818"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02818"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02819"
FT CONFLICT 32
FT /note="P -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 54982 MW; 3FA762DD78BD161A CRC64;
MPPSGPRAAL FLLPSLLLLR AVLAVPLERG APKEENPATE SPDTGLYYHR YLQEVINVLE
TDGHFREKLQ AANAEDIKSG KLSRELDFVS HHVRTKLDEL KRQEVSRLRM LLKAKMDAQQ
EPNIQLDHLN LLKQFEHLDP QNQHTFEARD LELLIQTATR DLAQYDAAHH EEFKRYEMLK
EHERRRYLES LGEEQRKEAE RKLEEQQRRH REHPKVNVPG SQAQLKEVWE ELDGLDPNRF
NPKTFFILHD INSDGVLDEQ ELEALFTKEL EKVYDPKNED DDMREMEEER LRMREHVMKN
VDTNQDRLVT LEEFLASTQR KEFGDTGEGW EQGKAGVPLP MAPVLTLQTV EMHPAYTEEE
LRRFEEELAA REAELNAKAQ RLSQETEALG RSQGRLEAQK RELQQAVLQM EQRKQQQQSH
NNPAPGPEGQ LKFHPDTDDV PVPAPAGDQK DVDASEKKVP EQTPEPPQLD SQHL
