NUCB1_PONAB
ID NUCB1_PONAB Reviewed; 463 AA.
AC Q5R4U1;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Nucleobindin-1;
DE Flags: Precursor;
GN Name=NUCB1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Major calcium-binding protein of the Golgi which may have a
CC role in calcium homeostasis (By similarity). 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:Q0P569,
CC ECO:0000250|UniProtKB:Q63083}.
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 -!- 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; CR861150; CAH93225.1; -; mRNA.
DR RefSeq; NP_001126897.1; NM_001133425.1.
DR AlphaFoldDB; Q5R4U1; -.
DR BMRB; Q5R4U1; -.
DR SMR; Q5R4U1; -.
DR STRING; 9601.ENSPPYP00000011431; -.
DR GeneID; 100173912; -.
DR KEGG; pon:100173912; -.
DR CTD; 4924; -.
DR eggNOG; KOG3866; Eukaryota.
DR InParanoid; Q5R4U1; -.
DR OrthoDB; 1339224at2759; -.
DR Proteomes; UP000001595; Unplaced.
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; IEA:InterPro.
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 2: Evidence at transcript level;
KW Calcium; Coiled coil; Cytoplasm; DNA-binding; Golgi apparatus;
KW Guanine-nucleotide releasing factor; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000250|UniProtKB:Q0P569"
FT CHAIN 27..463
FT /note="Nucleobindin-1"
FT /id="PRO_0000284128"
FT DOMAIN 240..275
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 292..327
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DNA_BIND 172..218
FT /evidence="ECO:0000255"
FT REGION 193..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..321
FT /note="Binds to GNAI2 and GNAI3"
FT /evidence="ECO:0000250"
FT REGION 368..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 150..218
FT /evidence="ECO:0000255"
FT COILED 341..409
FT /evidence="ECO:0000255"
FT MOTIF 303..333
FT /note="GBA"
FT /evidence="ECO:0000250|UniProtKB:Q02818"
FT COMPBIAS 193..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02818"
FT MOD_RES 148
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q02818"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02818"
SQ SEQUENCE 463 AA; 54063 MW; 4D052D467A1EED25 CRC64;
MPPSGPQGTL LLLPLLLLLL LRAVLAVPLE RGAPNKEETP ATESPDTGLY YHRYLQEVID
VLETDGHFRE KLQAANAEDI KSGKLSRELD FVSHHVRTKL DELKRQEVSR LRMLLKAKMD
AEQDPNVQVD HLNLLKQFEH LDPQNQHTFE ARDLELLIQT ATRDLAQYDA AHHEEFKRYE
MLKEHERRRY LESLGEEQRK EAERRLEEQQ RRHREHPKVN VPGSQAQLKE VWEELDGLDP
NRFNPKTFFI LHDINSDGVL DEQELEALFT KELEKVYDPK NEEDDMREME EERLRMREHV
MKNVDTNQDR LVTLGEFLAS TQRKEFGDTG EGWETVEMHP AYTEEELRRF EEELAAREAE
LNAKAQRLSQ ETEALGRSQG RLEAQKRELQ QAVLHMEQRK QQQQQQQQQG HKAPAAHPEG
QLKFHPDTDD VPVPAPAGDQ KEVDTSEKKL LERLPEVEVP QHL
