NECA1_RAT
ID NECA1_RAT Reviewed; 352 AA.
AC Q9ESB5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=N-terminal EF-hand calcium-binding protein 1;
DE Short=EF-hand calcium-binding protein 1;
DE AltName: Full=Neuronal calcium-binding protein 1;
DE AltName: Full=Synaptotagmin-interacting protein 1;
DE Short=Stip-1;
GN Name=Necab1; Synonyms=Efcbp1, Stip;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 315-321, AND INTERACTION
RP WITH STX1 AND CPNE6.
RC TISSUE=Brain;
RX PubMed=12044471; DOI=10.1016/s0306-4522(02)00063-5;
RA Sugita S., Ho A., Suedhof T.C.;
RT "NECABs: a family of neuronal Ca(2+)-binding proteins with an unusual
RT domain structure and a restricted expression pattern.";
RL Neuroscience 112:51-63(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- SUBUNIT: Interacts with STX1. May interact with CPNE6.
CC {ECO:0000250|UniProtKB:Q8N987}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR EMBL; AF193755; AAG28411.1; -; mRNA.
DR RefSeq; NP_071638.1; NM_022302.1.
DR AlphaFoldDB; Q9ESB5; -.
DR STRING; 10116.ENSRNOP00000009718; -.
DR iPTMnet; Q9ESB5; -.
DR PhosphoSitePlus; Q9ESB5; -.
DR PaxDb; Q9ESB5; -.
DR PRIDE; Q9ESB5; -.
DR GeneID; 64169; -.
DR KEGG; rno:64169; -.
DR UCSC; RGD:708548; rat.
DR CTD; 64168; -.
DR RGD; 708548; Necab1.
DR VEuPathDB; HostDB:ENSRNOG00000007256; -.
DR eggNOG; ENOG502QWRY; Eukaryota.
DR HOGENOM; CLU_041553_0_0_1; -.
DR InParanoid; Q9ESB5; -.
DR OMA; EVLLIQW; -.
DR OrthoDB; 924307at2759; -.
DR PhylomeDB; Q9ESB5; -.
DR PRO; PR:Q9ESB5; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000007256; Expressed in frontal cortex and 11 other tissues.
DR Genevisible; Q9ESB5; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0001835; P:blastocyst hatching; ISO:RGD.
DR GO; GO:0042984; P:regulation of amyloid precursor protein biosynthetic process; IBA:GO_Central.
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; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 2.
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; 2.
PE 1: Evidence at protein level;
KW Calcium; Coiled coil; Cytoplasm; Direct protein sequencing; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..352
FT /note="N-terminal EF-hand calcium-binding protein 1"
FT /id="PRO_0000282612"
FT DOMAIN 26..61
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 60..95
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 252..340
FT /note="ABM"
FT REGION 155..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 135..163
FT /evidence="ECO:0000255"
FT COILED 209..275
FT /evidence="ECO:0000255"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BG18"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BG18"
SQ SEQUENCE 352 AA; 40904 MW; 17D589374638F858 CRC64;
MEDSRETSPS SNNSSEELSS ALQLSKGMSI FLDILRRADK NDDGKLSFEE FKAYFADGVL
SGEELHELFH TIDTHNTNNL DTEELCEYFS QHLGEYENVL AALEDLNLSI LKAMGKTKKD
YQEASNLEQF VTRFLLKETL NQLQSLQNSL ECAMETTEEQ TRQERQGPSK PEVLSIQWPG
KRSSRRVQRH NSFSPNSPQF NVSSPALLEE DNQWMTQINR LQKLIDRLEK KDLKLEPLEE
EVIEENTKPH IMLVQRQMSV TEEDLEEFQL ALKHYVESAS AQSGCLRISI QKLSNESRYM
IYEFWENSSV WNRHLQTNYS KTFQRSNVDF LETPELTSTM LVPASWWILK NN
