ID   NECA3_BOVIN             Reviewed;         358 AA.
AC   A2VDW6;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=N-terminal EF-hand calcium-binding protein 3;
DE   AltName: Full=Amyloid-beta A4 protein-binding family A member 2-binding protein;
DE   AltName: Full=X11L-binding protein 51;
GN   Name=NECAB3; Synonyms=APBA2BP, XB51;
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 pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inhibits the interaction of APBA2 with amyloid-beta precursor
CC       protein (APP), and hence allows formation of amyloid-beta (By
CC       similarity). May enhance the activity of HIF1A and thus promote
CC       glycolysis under normoxic conditions; the function requires its ABM
CC       domain and may implicate the stabilization of the interaction between
CC       HIF1AN and APBA3 (By similarity). {ECO:0000250|UniProtKB:Q96P71}.
CC   -!- SUBUNIT: Interacts with the N-terminal domain of APBA2. Interacts with
CC       NEK2 (By similarity). Interacts with APBA3; APBA3 seems to mediate the
CC       interaction between NECAB3 and HIF1AN (By similarity).
CC       {ECO:0000250|UniProtKB:Q96P71}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q96P71}.
CC   -!- PTM: Phosphorylated by NEK2. {ECO:0000250|UniProtKB:Q96P71}.
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; BC133436; AAI33437.1; -; mRNA.
DR   RefSeq; NP_001075058.1; NM_001081589.2.
DR   AlphaFoldDB; A2VDW6; -.
DR   STRING; 9913.ENSBTAP00000005154; -.
DR   PaxDb; A2VDW6; -.
DR   GeneID; 514695; -.
DR   KEGG; bta:514695; -.
DR   CTD; 63941; -.
DR   eggNOG; ENOG502QWRY; Eukaryota.
DR   InParanoid; A2VDW6; -.
DR   OrthoDB; 924307at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR007138; ABM_dom.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR039862; NECAB1/2/3.
DR   PANTHER; PTHR12178; PTHR12178; 1.
DR   Pfam; PF03992; ABM; 1.
DR   Pfam; PF13202; EF-hand_5; 1.
DR   SMART; SM00054; EFh; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   SUPFAM; SSF54909; SSF54909; 1.
DR   PROSITE; PS51725; ABM; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Golgi apparatus; Metal-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..358
FT                   /note="N-terminal EF-hand calcium-binding protein 3"
FT                   /id="PRO_0000376933"
FT   DOMAIN          32..67
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          258..347
FT                   /note="ABM"
FT   REGION          159..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          177..186
FT                   /note="Required for interaction with APBA3"
FT                   /evidence="ECO:0000250|UniProtKB:Q96P71"
FT   COMPBIAS        168..182
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         45
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         47
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         49
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         51
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         56
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ   SEQUENCE   358 AA;  40154 MW;  697F002284A3B65B CRC64;
     MACAGLLTVC LIRPPAPEPP RPPAPAPAAG PAGHALFQDV FRRADKNDDG KLSFEEFQNY
     FADGVLSPGE LRELFSGVDG HPADNLETEK LCDYFSEHLG VYRPVLAALE SLNCAVLTAM
     DTTKLEYERA SKVDQFVTRF LLRETVSQLQ ALQSSLEGAS DTLEAQAQGP RSDEERVEVP
     SRPRGSRWAG RRALRSVSRS STWSPGSSNT GQSSEAEMQW RLQINRLQEL IDQLECKAPR
     LEPLHEEELT KGPSSHILVA QRQVQVAEEA LQDFHHALCC YVDFTGSQSH CLHVSAQKML
     DKASFTLYEF WQDEASWRRH QQSACSKAFQ RILIDHLRAP DTLTTVFFPA SWWIMNNN