NECA2_HUMAN
ID NECA2_HUMAN Reviewed; 386 AA.
AC Q7Z6G3; A2RRG3; H3BTW2; O75547; Q6ZSK0;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=N-terminal EF-hand calcium-binding protein 2;
DE Short=EF-hand calcium-binding protein 2;
DE AltName: Full=Neuronal calcium-binding protein 2;
DE AltName: Full=Synaptotagmin-interacting protein 2;
DE Short=Stip-2;
GN Name=NECAB2; Synonyms=EFCBP2;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Wu H., Yu L., Li D., Dang Y., Shan Y.;
RT "Cloning and characterization of human EFCBP1 and EFCBP2.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-386 (ISOFORM 1).
RC TISSUE=Subthalamic nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 170-386.
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 131-386, AND TISSUE SPECIFICITY.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 131-386.
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, INTERACTION WITH ADORA2A, AND SUBCELLULAR LOCATION.
RX PubMed=17689978; DOI=10.1016/j.mcn.2007.05.007;
RA Canela L., Lujan R., Lluis C., Burgueno J., Mallol J., Canela E.I.,
RA Franco R., Ciruela F.;
RT "The neuronal Ca(2+) -binding protein 2 (NECAB2) interacts with the
RT adenosine A(2A) receptor and modulates the cell surface expression and
RT function of the receptor.";
RL Mol. Cell. Neurosci. 36:1-12(2007).
RN [8]
RP FUNCTION, INTERACTION WITH GRM5, AND SUBCELLULAR LOCATION.
RX PubMed=19694902; DOI=10.1111/j.1471-4159.2009.06348.x;
RA Canela L., Fernandez-Duenas V., Albergaria C., Watanabe M., Lluis C.,
RA Mallol J., Canela E.I., Franco R., Lujan R., Ciruela F.;
RT "The association of metabotropic glutamate receptor type 5 with the
RT neuronal Ca2+-binding protein 2 modulates receptor function.";
RL J. Neurochem. 111:555-567(2009).
RN [9]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=26843217; DOI=10.1007/s00429-016-1191-3;
RA Zhang M.D., Barde S., Szodorai E., Josephson A., Mitsios N., Watanabe M.,
RA Attems J., Lubec G., Kovacs G.G., Uhlen M., Mulder J., Harkany T.,
RA Hoekfelt T.;
RT "Comparative anatomical distribution of neuronal calcium-binding protein
RT (NECAB) 1 and -2 in rodent and human spinal cord.";
RL Brain Struct. Funct. 221:3803-3823(2016).
CC -!- FUNCTION: May act as a signaling scaffold protein that senses
CC intracellular calcium. Can modulate ligand-induced internalization of
CC ADORA2A and coupling efficiency of mGluR5/GRM5; for both receptors may
CC regulate signaling activity such as promoting MAPK1/3 (ERK1/2)
CC activation. {ECO:0000305|PubMed:17689978, ECO:0000305|PubMed:19694902}.
CC -!- SUBUNIT: Interacts (calcium-dependent) with ADORA2A and GRM5.
CC {ECO:0000269|PubMed:17689978, ECO:0000269|PubMed:19694902}.
CC -!- INTERACTION:
CC Q7Z6G3; P29274: ADORA2A; NbExp=6; IntAct=EBI-950070, EBI-2902702;
CC Q7Z6G3; P41594-1: GRM5; NbExp=2; IntAct=EBI-950070, EBI-14039683;
CC Q7Z6G3-2; Q13155: AIMP2; NbExp=3; IntAct=EBI-10172876, EBI-745226;
CC Q7Z6G3-2; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-10172876, EBI-745073;
CC Q7Z6G3-2; Q00994: BEX3; NbExp=6; IntAct=EBI-10172876, EBI-741753;
CC Q7Z6G3-2; Q13895: BYSL; NbExp=6; IntAct=EBI-10172876, EBI-358049;
CC Q7Z6G3-2; Q9UFG5: C19orf25; NbExp=3; IntAct=EBI-10172876, EBI-741214;
CC Q7Z6G3-2; Q9NX04: C1orf109; NbExp=6; IntAct=EBI-10172876, EBI-8643161;
CC Q7Z6G3-2; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-10172876, EBI-747505;
CC Q7Z6G3-2; Q8TC20-4: CAGE1; NbExp=3; IntAct=EBI-10172876, EBI-11522698;
CC Q7Z6G3-2; Q9H257: CARD9; NbExp=3; IntAct=EBI-10172876, EBI-751319;
CC Q7Z6G3-2; Q8IYE0: CCDC146; NbExp=3; IntAct=EBI-10172876, EBI-10749669;
CC Q7Z6G3-2; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-10172876, EBI-10247802;
CC Q7Z6G3-2; Q494R4: CCDC153; NbExp=3; IntAct=EBI-10172876, EBI-10241443;
CC Q7Z6G3-2; Q16543: CDC37; NbExp=3; IntAct=EBI-10172876, EBI-295634;
CC Q7Z6G3-2; Q9BU64: CENPO; NbExp=3; IntAct=EBI-10172876, EBI-745954;
CC Q7Z6G3-2; Q9UER7: DAXX; NbExp=6; IntAct=EBI-10172876, EBI-77321;
CC Q7Z6G3-2; Q9BY27: DGCR6L; NbExp=3; IntAct=EBI-10172876, EBI-742953;
CC Q7Z6G3-2; Q96EV8: DTNBP1; NbExp=3; IntAct=EBI-10172876, EBI-465804;
CC Q7Z6G3-2; Q13409-3: DYNC1I2; NbExp=3; IntAct=EBI-10172876, EBI-12094038;
CC Q7Z6G3-2; Q08426: EHHADH; NbExp=3; IntAct=EBI-10172876, EBI-2339219;
CC Q7Z6G3-2; O60573: EIF4E2; NbExp=3; IntAct=EBI-10172876, EBI-398610;
CC Q7Z6G3-2; Q3B820: FAM161A; NbExp=3; IntAct=EBI-10172876, EBI-719941;
CC Q7Z6G3-2; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-10172876, EBI-7225287;
CC Q7Z6G3-2; Q96CN9: GCC1; NbExp=3; IntAct=EBI-10172876, EBI-746252;
CC Q7Z6G3-2; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-10172876, EBI-2514791;
CC Q7Z6G3-2; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-10172876, EBI-14103818;
CC Q7Z6G3-2; A5PKX9: INADL; NbExp=3; IntAct=EBI-10172876, EBI-12035052;
CC Q7Z6G3-2; Q9NVR2: INTS10; NbExp=3; IntAct=EBI-10172876, EBI-536703;
CC Q7Z6G3-2; Q9H1K1: ISCU; NbExp=3; IntAct=EBI-10172876, EBI-1047335;
CC Q7Z6G3-2; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-10172876, EBI-2556193;
CC Q7Z6G3-2; Q7Z3B3: KANSL1; NbExp=3; IntAct=EBI-10172876, EBI-740244;
CC Q7Z6G3-2; O60341: KDM1A; NbExp=3; IntAct=EBI-10172876, EBI-710124;
CC Q7Z6G3-2; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-10172876, EBI-2125614;
CC Q7Z6G3-2; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-10172876, EBI-14069005;
CC Q7Z6G3-2; Q6P597: KLC3; NbExp=3; IntAct=EBI-10172876, EBI-1643885;
CC Q7Z6G3-2; Q9NSK0: KLC4; NbExp=6; IntAct=EBI-10172876, EBI-949319;
CC Q7Z6G3-2; P52292: KPNA2; NbExp=3; IntAct=EBI-10172876, EBI-349938;
CC Q7Z6G3-2; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-10172876, EBI-726510;
CC Q7Z6G3-2; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-10172876, EBI-739832;
CC Q7Z6G3-2; Q92552-2: MRPS27; NbExp=3; IntAct=EBI-10172876, EBI-10278573;
CC Q7Z6G3-2; A6NI15: MSGN1; NbExp=3; IntAct=EBI-10172876, EBI-11991020;
CC Q7Z6G3-2; Q96QG7: MTMR9; NbExp=3; IntAct=EBI-10172876, EBI-744593;
CC Q7Z6G3-2; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-10172876, EBI-2858213;
CC Q7Z6G3-2; Q8N987: NECAB1; NbExp=3; IntAct=EBI-10172876, EBI-11956853;
CC Q7Z6G3-2; Q7Z6G3-2: NECAB2; NbExp=6; IntAct=EBI-10172876, EBI-10172876;
CC Q7Z6G3-2; Q9HC98: NEK6; NbExp=3; IntAct=EBI-10172876, EBI-740364;
CC Q7Z6G3-2; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-10172876, EBI-11750983;
CC Q7Z6G3-2; Q9Y221: NIP7; NbExp=3; IntAct=EBI-10172876, EBI-749003;
CC Q7Z6G3-2; Q96HA8: NTAQ1; NbExp=8; IntAct=EBI-10172876, EBI-741158;
CC Q7Z6G3-2; A5D8V7: ODAD3; NbExp=3; IntAct=EBI-10172876, EBI-8466445;
CC Q7Z6G3-2; A5D8V7-2: ODAD3; NbExp=3; IntAct=EBI-10172876, EBI-10173824;
CC Q7Z6G3-2; Q96NG3: ODAD4; NbExp=3; IntAct=EBI-10172876, EBI-1046387;
CC Q7Z6G3-2; O43482: OIP5; NbExp=6; IntAct=EBI-10172876, EBI-536879;
CC Q7Z6G3-2; Q15154-3: PCM1; NbExp=5; IntAct=EBI-10172876, EBI-11742977;
CC Q7Z6G3-2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-10172876, EBI-79165;
CC Q7Z6G3-2; P54646: PRKAA2; NbExp=3; IntAct=EBI-10172876, EBI-1383852;
CC Q7Z6G3-2; Q99633: PRPF18; NbExp=3; IntAct=EBI-10172876, EBI-2798416;
CC Q7Z6G3-2; Q3MIT2: PUS10; NbExp=3; IntAct=EBI-10172876, EBI-11983583;
CC Q7Z6G3-2; Q9P2K3: RCOR3; NbExp=3; IntAct=EBI-10172876, EBI-743428;
CC Q7Z6G3-2; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-10172876, EBI-1504830;
CC Q7Z6G3-2; Q9NPQ8-4: RIC8A; NbExp=3; IntAct=EBI-10172876, EBI-9091816;
CC Q7Z6G3-2; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-10172876, EBI-11984663;
CC Q7Z6G3-2; Q06455-4: RUNX1T1; NbExp=3; IntAct=EBI-10172876, EBI-10224192;
CC Q7Z6G3-2; O00560: SDCBP; NbExp=5; IntAct=EBI-10172876, EBI-727004;
CC Q7Z6G3-2; Q9H788: SH2D4A; NbExp=6; IntAct=EBI-10172876, EBI-747035;
CC Q7Z6G3-2; Q9H788-2: SH2D4A; NbExp=3; IntAct=EBI-10172876, EBI-10308083;
CC Q7Z6G3-2; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-10172876, EBI-358489;
CC Q7Z6G3-2; O95295: SNAPIN; NbExp=3; IntAct=EBI-10172876, EBI-296723;
CC Q7Z6G3-2; O94964-4: SOGA1; NbExp=3; IntAct=EBI-10172876, EBI-14083835;
CC Q7Z6G3-2; A1L4H1: SSC5D; NbExp=6; IntAct=EBI-10172876, EBI-10172867;
CC Q7Z6G3-2; Q15560: TCEA2; NbExp=3; IntAct=EBI-10172876, EBI-710310;
CC Q7Z6G3-2; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-10172876, EBI-11523345;
CC Q7Z6G3-2; Q8IWR1: TRIM59; NbExp=3; IntAct=EBI-10172876, EBI-10262539;
CC Q7Z6G3-2; Q8N7C3: TRIML2; NbExp=4; IntAct=EBI-10172876, EBI-11059915;
CC Q7Z6G3-2; P02766: TTR; NbExp=3; IntAct=EBI-10172876, EBI-711909;
CC Q7Z6G3-2; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-10172876, EBI-739895;
CC Q7Z6G3-2; Q8N720: ZNF655; NbExp=3; IntAct=EBI-10172876, EBI-625509;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:F1LQY6,
CC ECO:0000250|UniProtKB:Q91ZP9}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:F1LQY6}. Cell projection, axon
CC {ECO:0000250|UniProtKB:F1LQY6}. Cell membrane
CC {ECO:0000269|PubMed:17689978, ECO:0000269|PubMed:19694902}.
CC Note=Colocalizes with ADORA2A and/or mGluR5/GRM5 at the plasma membrane
CC (PubMed:17689978, PubMed:19694902). Found in neuronal somata
CC (PubMed:26843217). Detected in the cytoplasm of striatal neurons, at
CC postsynaptic sites, filling dendritic shafts and spines, and at
CC presynaptic sites, filling axon terminals (By similarity).
CC {ECO:0000250|UniProtKB:F1LQY6, ECO:0000269|PubMed:17689978,
CC ECO:0000269|PubMed:19694902, ECO:0000269|PubMed:26843217}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z6G3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z6G3-2; Sequence=VSP_058936;
CC -!- TISSUE SPECIFICITY: Expressed in brain. Expressed in the spinal dorsal
CC horn with especially strong expression in lamina IIi; found in excitory
CC synaptic boutons and in ependymal cells (at protein level).
CC {ECO:0000269|PubMed:12044471, ECO:0000269|PubMed:26843217}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI31616.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC86948.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY299331; AAP57260.1; -; mRNA.
DR EMBL; AK127376; BAC86948.1; ALT_INIT; mRNA.
DR EMBL; AC040169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016979; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC131615; AAI31616.1; ALT_INIT; mRNA.
DR EMBL; AF193758; AAG28414.1; -; mRNA.
DR EMBL; AF070637; AAC25392.1; -; mRNA.
DR CCDS; CCDS10940.1; -. [Q7Z6G3-1]
DR CCDS; CCDS82019.1; -. [Q7Z6G3-2]
DR RefSeq; NP_001316678.1; NM_001329749.1. [Q7Z6G3-2]
DR RefSeq; NP_061938.2; NM_019065.2. [Q7Z6G3-1]
DR AlphaFoldDB; Q7Z6G3; -.
DR SMR; Q7Z6G3; -.
DR BioGRID; 120035; 112.
DR IntAct; Q7Z6G3; 94.
DR MINT; Q7Z6G3; -.
DR STRING; 9606.ENSP00000307449; -.
DR PhosphoSitePlus; Q7Z6G3; -.
DR BioMuta; NECAB2; -.
DR DMDM; 74762441; -.
DR MassIVE; Q7Z6G3; -.
DR PaxDb; Q7Z6G3; -.
DR PeptideAtlas; Q7Z6G3; -.
DR PRIDE; Q7Z6G3; -.
DR ProteomicsDB; 42754; -.
DR ProteomicsDB; 69400; -.
DR Antibodypedia; 2918; 115 antibodies from 22 providers.
DR DNASU; 54550; -.
DR Ensembl; ENST00000305202.9; ENSP00000307449.4; ENSG00000103154.10. [Q7Z6G3-1]
DR Ensembl; ENST00000565691.5; ENSP00000457354.1; ENSG00000103154.10. [Q7Z6G3-2]
DR GeneID; 54550; -.
DR KEGG; hsa:54550; -.
DR MANE-Select; ENST00000305202.9; ENSP00000307449.4; NM_019065.3; NP_061938.2.
DR UCSC; uc002fhd.4; human. [Q7Z6G3-1]
DR CTD; 54550; -.
DR DisGeNET; 54550; -.
DR GeneCards; NECAB2; -.
DR HGNC; HGNC:23746; NECAB2.
DR HPA; ENSG00000103154; Tissue enriched (brain).
DR MIM; 618130; gene.
DR neXtProt; NX_Q7Z6G3; -.
DR OpenTargets; ENSG00000103154; -.
DR PharmGKB; PA162397412; -.
DR VEuPathDB; HostDB:ENSG00000103154; -.
DR eggNOG; ENOG502QRUC; Eukaryota.
DR GeneTree; ENSGT00950000183131; -.
DR InParanoid; Q7Z6G3; -.
DR OMA; ARHYPSK; -.
DR OrthoDB; 924307at2759; -.
DR PhylomeDB; Q7Z6G3; -.
DR TreeFam; TF331029; -.
DR PathwayCommons; Q7Z6G3; -.
DR SignaLink; Q7Z6G3; -.
DR BioGRID-ORCS; 54550; 9 hits in 1062 CRISPR screens.
DR GeneWiki; EFCBP2; -.
DR GenomeRNAi; 54550; -.
DR Pharos; Q7Z6G3; Tbio.
DR PRO; PR:Q7Z6G3; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q7Z6G3; protein.
DR Bgee; ENSG00000103154; Expressed in nucleus accumbens and 154 other tissues.
DR ExpressionAtlas; Q7Z6G3; baseline and differential.
DR Genevisible; Q7Z6G3; HS.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031687; F:A2A adenosine receptor binding; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; IDA:UniProtKB.
DR GO; GO:1904021; P:negative regulation of G protein-coupled receptor internalization; IDA:UniProtKB.
DR GO; GO:0060168; P:positive regulation of adenosine receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:1900451; P:positive regulation of glutamate receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:1905477; P:positive regulation of protein localization to membrane; IDA:UniProtKB.
DR GO; GO:0042984; P:regulation of amyloid precursor protein biosynthetic process; IBA:GO_Central.
DR CDD; cd00051; EFh; 1.
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; 2.
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; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cell projection; Coiled coil;
KW Cytoplasm; Membrane; Metal-binding; Methylation; Reference proteome;
KW Repeat.
FT CHAIN 1..386
FT /note="N-terminal EF-hand calcium-binding protein 2"
FT /id="PRO_0000282613"
FT DOMAIN 60..95
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 96..129
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 286..375
FT /note="ABM"
FT COILED 170..201
FT /evidence="ECO:0000255"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 10
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q91ZP9"
FT MOD_RES 42
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q91ZP9"
FT VAR_SEQ 1..121
FT /note="MCERAARLCRAGAHRLLREPPQQGRALGGLLRWVGARMGEPRESLAPAAPAD
FT PGPASPRGGTAVILDIFRRADKNDDGKLSLEEFQLFFADGVLNEKELEDLFHTIDSDNT
FT NHVDTKELCD -> MMMGSCPWRNSSSSLQMASLMRKNWRISFTRLTLTTPN (in
FT isoform 2)"
FT /id="VSP_058936"
FT VARIANT 233
FT /note="G -> S (in dbSNP:rs2292323)"
FT /id="VAR_048639"
FT VARIANT 235
FT /note="T -> S (in dbSNP:rs2292324)"
FT /id="VAR_048640"
FT VARIANT 308
FT /note="Q -> H (in dbSNP:rs2292329)"
FT /id="VAR_048641"
FT VARIANT 353
FT /note="L -> V (in dbSNP:rs2271298)"
FT /id="VAR_048642"
SQ SEQUENCE 386 AA; 43194 MW; D5F32B9AACF1A1C1 CRC64;
MCERAARLCR AGAHRLLREP PQQGRALGGL LRWVGARMGE PRESLAPAAP ADPGPASPRG
GTAVILDIFR RADKNDDGKL SLEEFQLFFA DGVLNEKELE DLFHTIDSDN TNHVDTKELC
DYFVDHMGDY EDVLASLETL NHSVLKAMGY TKKVYEGGSN VDQFVTRFLL KETANQIQSL
LSSVESAVEA IEEQTSQLRQ NHIKPSHSAA QTWCGSPTPA SAPNHKLMAM EQGKTLPSAT
EDAKEEGLEA QISRLAELIG RLESKALWFD LQQRLSDEDG TNMHLQLVRQ EMAVCPEQLS
EFLDSLRQYL RGTTGVRNCF HITAVRLSDG FTFVIYEFWE TEEAWKRHLQ SPLCKAFRHV
KVDTLSQPEA LSRILVPAAW CTVGRD
