Full text data of NUCB2
NUCB2
(NEFA)
[Confidence: high (present in two of the MS resources)]
Nucleobindin-2 (DNA-binding protein NEFA; Gastric cancer antigen Zg4; Prepronesfatin; Nesfatin-1; Flags: Precursor)
Nucleobindin-2 (DNA-binding protein NEFA; Gastric cancer antigen Zg4; Prepronesfatin; Nesfatin-1; Flags: Precursor)
Comments
Isoform P80303-2 was detected.
Isoform P80303-2 was detected.
UniProt
P80303
ID NUCB2_HUMAN Reviewed; 420 AA.
AC P80303; A8K642; D3DQX5; Q8NFT5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-MAR-2009, sequence version 2.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Nucleobindin-2;
DE AltName: Full=DNA-binding protein NEFA;
DE AltName: Full=Gastric cancer antigen Zg4;
DE AltName: Full=Prepronesfatin;
DE Contains:
DE RecName: Full=Nesfatin-1;
DE Flags: Precursor;
GN Name=NUCB2; Synonyms=NEFA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP VARIANT ASN-303.
RC TISSUE=Blood;
RX PubMed=7811391;
RA Barnikol-Watanabe S., Gross N.A., Goetz H., Henkel T., Karabinos A.,
RA Kratzin H., Barnikol H.U., Hilschmann N.;
RT "Human protein NEFA, a novel DNA binding/EF-hand/leucine zipper
RT protein. Molecular cloning and sequence analysis of the cDNA,
RT isolation and characterization of the protein.";
RL Biol. Chem. Hoppe-Seyler 375:497-512(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASN-303.
RX PubMed=9639681; DOI=10.1016/S0925-4439(98)00025-8;
RA Deangelis M.M., Doucet J.P., Drury S., Sherry S.T., Robichaux M.B.,
RA Den Z., Pelias M.Z., Ditta G.M., Keats B.J., Deininger P.L.,
RA Batzer M.A.;
RT "Assembly of a high-resolution map of the Acadian Usher syndrome
RT region and localization of the nuclear EF-hand acidic gene.";
RL Biochim. Biophys. Acta 1407:84-91(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP VARIANTS ASN-303 AND GLN-402 DEL.
RX PubMed=12087473; DOI=10.1038/sj.bjc.6600321;
RA Line A., Stengrevics A., Slucka Z., Li G., Jankevics E., Rees R.C.;
RT "Serological identification and expression analysis of gastric cancer-
RT associated genes.";
RL Br. J. Cancer 86:1824-1830(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-303.
RX PubMed=20427483; DOI=10.1210/en.2009-1169;
RA Yamada M., Horiguchi K., Umezawa R., Hashimoto K., Satoh T., Ozawa A.,
RA Shibusawa N., Monden T., Okada S., Shimizu H., Mori M.;
RT "Troglitazone, a ligand of peroxisome proliferator-activated receptor-
RT gamma, stabilizes NUCB2 (Nesfatin) mRNA by activating the ERK1/2
RT pathway: isolation and characterization of the human NUCB2 gene.";
RL Endocrinology 151:2494-2503(2010).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
RP ASN-303 AND GLN-402 DEL.
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-303.
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=11749975; DOI=10.1016/S0014-5793(01)03187-8;
RA Nesselhut J., Jurgan U., Onken E., Gotz H., Barnikol H.U.,
RA Hirschfeld G., Barnikol-Watanabe S., Hilschmann N.;
RT "Golgi retention of human protein NEFA is mediated by its N-terminal
RT Leu/Ile-rich region.";
RL FEBS Lett. 509:469-475(2001).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-303, AND MASS SPECTROMETRY.
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Calcium-binding protein. May have a role in calcium
CC homeostasis.
CC -!- FUNCTION: Nesfatin-1: Anorexigenic peptide, seems to play an
CC important role in hypothalamic pathways regulating food intake and
CC energy homeostasis, acting in a leptin-independent manner. May
CC also exert hypertensive roles and modulate blood pressure through
CC directly acting on peripheral arterial resistance (By similarity).
CC -!- INTERACTION:
CC P24522:GADD45A; NbExp=2; IntAct=EBI-2296670, EBI-448167;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Membrane; Peripheral
CC membrane protein. Cytoplasm. Secreted. Endoplasmic reticulum (By
CC similarity). Nucleus envelope (By similarity). Note=Golgi
CC retention is mediated by its N-terminal region.
CC -!- SUBCELLULAR LOCATION: Nesfatin-1: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P80303-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P80303-2; Sequence=VSP_036450;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in spleen, testis and
CC normal stomach.
CC -!- POLYMORPHISM: Deletion of Gln-402 is frequent.
CC -!- MISCELLANEOUS: NEFA stands for N=DNA-binding; EF=EF-hand; A=Acidic
CC region.
CC -!- SIMILARITY: Belongs to the nucleobindin family.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
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DR EMBL; X76732; CAA54148.1; -; mRNA.
DR EMBL; AF052642; AAC06300.1; -; mRNA.
DR EMBL; AF052643; AAC06301.1; -; mRNA.
DR EMBL; AF052644; AAC06302.1; -; mRNA.
DR EMBL; AF450266; AAM73810.1; -; mRNA.
DR EMBL; AB478625; BAJ09615.1; -; Genomic_DNA.
DR EMBL; AK291507; BAF84196.1; -; mRNA.
DR EMBL; AC107956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68439.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68440.1; -; Genomic_DNA.
DR PIR; S55272; S55272.
DR RefSeq; NP_005004.1; NM_005013.2.
DR RefSeq; XP_005252998.1; XM_005252941.1.
DR RefSeq; XP_005252999.1; XM_005252942.1.
DR RefSeq; XP_005253000.1; XM_005252943.1.
DR RefSeq; XP_005253001.1; XM_005252944.1.
DR RefSeq; XP_005253002.1; XM_005252945.1.
DR RefSeq; XP_005253003.1; XM_005252946.1.
DR RefSeq; XP_005253004.1; XM_005252947.1.
DR RefSeq; XP_005253005.1; XM_005252948.1.
DR UniGene; Hs.654599; -.
DR ProteinModelPortal; P80303; -.
DR SMR; P80303; 229-327.
DR IntAct; P80303; 11.
DR MINT; MINT-2804938; -.
DR STRING; 9606.ENSP00000320168; -.
DR PhosphoSite; P80303; -.
DR DMDM; 224471846; -.
DR PaxDb; P80303; -.
DR PRIDE; P80303; -.
DR Ensembl; ENST00000323688; ENSP00000320168; ENSG00000070081.
DR Ensembl; ENST00000529010; ENSP00000436455; ENSG00000070081.
DR GeneID; 4925; -.
DR KEGG; hsa:4925; -.
DR UCSC; uc001mms.1; human.
DR CTD; 4925; -.
DR GeneCards; GC11P017229; -.
DR HGNC; HGNC:8044; NUCB2.
DR HPA; CAB015931; -.
DR HPA; HPA008395; -.
DR MIM; 608020; gene.
DR neXtProt; NX_P80303; -.
DR PharmGKB; PA31826; -.
DR eggNOG; NOG262100; -.
DR HOGENOM; HOG000007216; -.
DR HOVERGEN; HBG052685; -.
DR InParanoid; P80303; -.
DR OMA; DHPKVNH; -.
DR ChiTaRS; NUCB2; human.
DR GeneWiki; NUCB2; -.
DR GenomeRNAi; 4925; -.
DR NextBio; 18967; -.
DR PMAP-CutDB; P80303; -.
DR PRO; PR:P80303; -.
DR ArrayExpress; P80303; -.
DR Bgee; P80303; -.
DR CleanEx; HS_NUCB2; -.
DR Genevestigator; P80303; -.
DR GO; GO:0005829; C:cytosol; TAS:ProtInc.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005640; C:nuclear outer membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cleavage on pair of basic residues;
KW Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Endoplasmic reticulum; Golgi apparatus; Membrane; Metal-binding;
KW Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1 24 Potential.
FT CHAIN 25 420 Nucleobindin-2.
FT /FTId=PRO_0000004165.
FT CHAIN 25 106 Nesfatin-1.
FT /FTId=PRO_0000419819.
FT DOMAIN 241 276 EF-hand 1.
FT DOMAIN 293 328 EF-hand 2.
FT DNA_BIND 171 223 By similarity.
FT CA_BIND 254 265 1.
FT CA_BIND 306 317 2.
FT REGION 213 420 Binds to necdin (By similarity).
FT COMPBIAS 282 293 Asp/Glu-rich (acidic).
FT MOD_RES 257 257 Phosphoserine.
FT MOD_RES 332 332 Phosphoserine.
FT VAR_SEQ 419 420 HI -> RV (in isoform 2).
FT /FTId=VSP_036450.
FT VARIANT 303 303 S -> N (in dbSNP:rs2521998).
FT /FTId=VAR_068746.
FT VARIANT 338 338 Q -> E (in dbSNP:rs757081).
FT /FTId=VAR_024399.
FT VARIANT 402 402 Missing.
FT /FTId=VAR_020923.
FT CONFLICT 150 150 F -> L (in Ref. 5; BAF84196).
SQ SEQUENCE 420 AA; 50196 MW; 5BA7459AB725A1A3 CRC64;
MRWRTILLQY CFLLITCLLT ALEAVPIDID KTKVQNIHPV ESAKIEPPDT GLYYDEYLKQ
VIDVLETDKH FREKLQKADI EEIKSGRLSK ELDLVSHHVR TKLDELKRQE VGRLRMLIKA
KLDSLQDIGM DHQALLKQFD HLNHLNPDKF ESTDLDMLIK AATSDLEHYD KTRHEEFKKY
EMMKEHERRE YLKTLNEEKR KEEESKFEEM KKKHENHPKV NHPGSKDQLK EVWEETDGLD
PNDFDPKTFF KLHDVNSDGF LDEQELEALF TKELEKVYDP KNEEDDMVEM EEERLRMREH
VMSEVDTNKD RLVTLEEFLK ATEKKEFLEP DSWETLDQQQ FFTEEELKEY ENIIALQENE
LKKKADELQK QKEELQRQHD QLEAQKLEYH QVIQQMEQKK LQQGIPPSGP AGELKFEPHI
//
ID NUCB2_HUMAN Reviewed; 420 AA.
AC P80303; A8K642; D3DQX5; Q8NFT5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-MAR-2009, sequence version 2.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Nucleobindin-2;
DE AltName: Full=DNA-binding protein NEFA;
DE AltName: Full=Gastric cancer antigen Zg4;
DE AltName: Full=Prepronesfatin;
DE Contains:
DE RecName: Full=Nesfatin-1;
DE Flags: Precursor;
GN Name=NUCB2; Synonyms=NEFA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP VARIANT ASN-303.
RC TISSUE=Blood;
RX PubMed=7811391;
RA Barnikol-Watanabe S., Gross N.A., Goetz H., Henkel T., Karabinos A.,
RA Kratzin H., Barnikol H.U., Hilschmann N.;
RT "Human protein NEFA, a novel DNA binding/EF-hand/leucine zipper
RT protein. Molecular cloning and sequence analysis of the cDNA,
RT isolation and characterization of the protein.";
RL Biol. Chem. Hoppe-Seyler 375:497-512(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASN-303.
RX PubMed=9639681; DOI=10.1016/S0925-4439(98)00025-8;
RA Deangelis M.M., Doucet J.P., Drury S., Sherry S.T., Robichaux M.B.,
RA Den Z., Pelias M.Z., Ditta G.M., Keats B.J., Deininger P.L.,
RA Batzer M.A.;
RT "Assembly of a high-resolution map of the Acadian Usher syndrome
RT region and localization of the nuclear EF-hand acidic gene.";
RL Biochim. Biophys. Acta 1407:84-91(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP VARIANTS ASN-303 AND GLN-402 DEL.
RX PubMed=12087473; DOI=10.1038/sj.bjc.6600321;
RA Line A., Stengrevics A., Slucka Z., Li G., Jankevics E., Rees R.C.;
RT "Serological identification and expression analysis of gastric cancer-
RT associated genes.";
RL Br. J. Cancer 86:1824-1830(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-303.
RX PubMed=20427483; DOI=10.1210/en.2009-1169;
RA Yamada M., Horiguchi K., Umezawa R., Hashimoto K., Satoh T., Ozawa A.,
RA Shibusawa N., Monden T., Okada S., Shimizu H., Mori M.;
RT "Troglitazone, a ligand of peroxisome proliferator-activated receptor-
RT gamma, stabilizes NUCB2 (Nesfatin) mRNA by activating the ERK1/2
RT pathway: isolation and characterization of the human NUCB2 gene.";
RL Endocrinology 151:2494-2503(2010).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
RP ASN-303 AND GLN-402 DEL.
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-303.
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=11749975; DOI=10.1016/S0014-5793(01)03187-8;
RA Nesselhut J., Jurgan U., Onken E., Gotz H., Barnikol H.U.,
RA Hirschfeld G., Barnikol-Watanabe S., Hilschmann N.;
RT "Golgi retention of human protein NEFA is mediated by its N-terminal
RT Leu/Ile-rich region.";
RL FEBS Lett. 509:469-475(2001).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-303, AND MASS SPECTROMETRY.
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Calcium-binding protein. May have a role in calcium
CC homeostasis.
CC -!- FUNCTION: Nesfatin-1: Anorexigenic peptide, seems to play an
CC important role in hypothalamic pathways regulating food intake and
CC energy homeostasis, acting in a leptin-independent manner. May
CC also exert hypertensive roles and modulate blood pressure through
CC directly acting on peripheral arterial resistance (By similarity).
CC -!- INTERACTION:
CC P24522:GADD45A; NbExp=2; IntAct=EBI-2296670, EBI-448167;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Membrane; Peripheral
CC membrane protein. Cytoplasm. Secreted. Endoplasmic reticulum (By
CC similarity). Nucleus envelope (By similarity). Note=Golgi
CC retention is mediated by its N-terminal region.
CC -!- SUBCELLULAR LOCATION: Nesfatin-1: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P80303-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P80303-2; Sequence=VSP_036450;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in spleen, testis and
CC normal stomach.
CC -!- POLYMORPHISM: Deletion of Gln-402 is frequent.
CC -!- MISCELLANEOUS: NEFA stands for N=DNA-binding; EF=EF-hand; A=Acidic
CC region.
CC -!- SIMILARITY: Belongs to the nucleobindin family.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
CC -----------------------------------------------------------------------
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DR EMBL; X76732; CAA54148.1; -; mRNA.
DR EMBL; AF052642; AAC06300.1; -; mRNA.
DR EMBL; AF052643; AAC06301.1; -; mRNA.
DR EMBL; AF052644; AAC06302.1; -; mRNA.
DR EMBL; AF450266; AAM73810.1; -; mRNA.
DR EMBL; AB478625; BAJ09615.1; -; Genomic_DNA.
DR EMBL; AK291507; BAF84196.1; -; mRNA.
DR EMBL; AC107956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68439.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68440.1; -; Genomic_DNA.
DR PIR; S55272; S55272.
DR RefSeq; NP_005004.1; NM_005013.2.
DR RefSeq; XP_005252998.1; XM_005252941.1.
DR RefSeq; XP_005252999.1; XM_005252942.1.
DR RefSeq; XP_005253000.1; XM_005252943.1.
DR RefSeq; XP_005253001.1; XM_005252944.1.
DR RefSeq; XP_005253002.1; XM_005252945.1.
DR RefSeq; XP_005253003.1; XM_005252946.1.
DR RefSeq; XP_005253004.1; XM_005252947.1.
DR RefSeq; XP_005253005.1; XM_005252948.1.
DR UniGene; Hs.654599; -.
DR ProteinModelPortal; P80303; -.
DR SMR; P80303; 229-327.
DR IntAct; P80303; 11.
DR MINT; MINT-2804938; -.
DR STRING; 9606.ENSP00000320168; -.
DR PhosphoSite; P80303; -.
DR DMDM; 224471846; -.
DR PaxDb; P80303; -.
DR PRIDE; P80303; -.
DR Ensembl; ENST00000323688; ENSP00000320168; ENSG00000070081.
DR Ensembl; ENST00000529010; ENSP00000436455; ENSG00000070081.
DR GeneID; 4925; -.
DR KEGG; hsa:4925; -.
DR UCSC; uc001mms.1; human.
DR CTD; 4925; -.
DR GeneCards; GC11P017229; -.
DR HGNC; HGNC:8044; NUCB2.
DR HPA; CAB015931; -.
DR HPA; HPA008395; -.
DR MIM; 608020; gene.
DR neXtProt; NX_P80303; -.
DR PharmGKB; PA31826; -.
DR eggNOG; NOG262100; -.
DR HOGENOM; HOG000007216; -.
DR HOVERGEN; HBG052685; -.
DR InParanoid; P80303; -.
DR OMA; DHPKVNH; -.
DR ChiTaRS; NUCB2; human.
DR GeneWiki; NUCB2; -.
DR GenomeRNAi; 4925; -.
DR NextBio; 18967; -.
DR PMAP-CutDB; P80303; -.
DR PRO; PR:P80303; -.
DR ArrayExpress; P80303; -.
DR Bgee; P80303; -.
DR CleanEx; HS_NUCB2; -.
DR Genevestigator; P80303; -.
DR GO; GO:0005829; C:cytosol; TAS:ProtInc.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005640; C:nuclear outer membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cleavage on pair of basic residues;
KW Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Endoplasmic reticulum; Golgi apparatus; Membrane; Metal-binding;
KW Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1 24 Potential.
FT CHAIN 25 420 Nucleobindin-2.
FT /FTId=PRO_0000004165.
FT CHAIN 25 106 Nesfatin-1.
FT /FTId=PRO_0000419819.
FT DOMAIN 241 276 EF-hand 1.
FT DOMAIN 293 328 EF-hand 2.
FT DNA_BIND 171 223 By similarity.
FT CA_BIND 254 265 1.
FT CA_BIND 306 317 2.
FT REGION 213 420 Binds to necdin (By similarity).
FT COMPBIAS 282 293 Asp/Glu-rich (acidic).
FT MOD_RES 257 257 Phosphoserine.
FT MOD_RES 332 332 Phosphoserine.
FT VAR_SEQ 419 420 HI -> RV (in isoform 2).
FT /FTId=VSP_036450.
FT VARIANT 303 303 S -> N (in dbSNP:rs2521998).
FT /FTId=VAR_068746.
FT VARIANT 338 338 Q -> E (in dbSNP:rs757081).
FT /FTId=VAR_024399.
FT VARIANT 402 402 Missing.
FT /FTId=VAR_020923.
FT CONFLICT 150 150 F -> L (in Ref. 5; BAF84196).
SQ SEQUENCE 420 AA; 50196 MW; 5BA7459AB725A1A3 CRC64;
MRWRTILLQY CFLLITCLLT ALEAVPIDID KTKVQNIHPV ESAKIEPPDT GLYYDEYLKQ
VIDVLETDKH FREKLQKADI EEIKSGRLSK ELDLVSHHVR TKLDELKRQE VGRLRMLIKA
KLDSLQDIGM DHQALLKQFD HLNHLNPDKF ESTDLDMLIK AATSDLEHYD KTRHEEFKKY
EMMKEHERRE YLKTLNEEKR KEEESKFEEM KKKHENHPKV NHPGSKDQLK EVWEETDGLD
PNDFDPKTFF KLHDVNSDGF LDEQELEALF TKELEKVYDP KNEEDDMVEM EEERLRMREH
VMSEVDTNKD RLVTLEEFLK ATEKKEFLEP DSWETLDQQQ FFTEEELKEY ENIIALQENE
LKKKADELQK QKEELQRQHD QLEAQKLEYH QVIQQMEQKK LQQGIPPSGP AGELKFEPHI
//
MIM
608020
*RECORD*
*FIELD* NO
608020
*FIELD* TI
*608020 NUCLEOBINDIN 2; NUCB2
;;NEFA
*FIELD* TX
DESCRIPTION
Nucleobindin-2 is a calcium-binding EF-hand protein.
read more
CLONING
By screening cDNA libraries constructed from a human acute lymphoblastic
leukemia cell line with an anti-CALLA (120520) monoclonal antibody,
Barnikol-Watanabe et al. (1994) isolated a partial NUCB2 cDNA clone.
They assembled a full-length clone encoding a deduced 420-amino acid
protein, which they called NEFA, with a calculated molecular mass of 48
kD. The protein contains a basic amino acid-rich putative DNA-binding
domain with a potential nuclear targeting signal, 2 helix-loop-helix
motif regions, 2 concurrent EF-hand motifs, an acidic amino acid region
between the EF-hands, and a leucine zipper motif. The protein shares
high homology with human NUCB1 (601323). Isoelectric focusing
demonstrated the presence of NUCB2 on the plasma membrane, in the
cytosol, and in the culture supernatant. NUCB2 is a highly charged
protein with a relative molecular mass of 55 kD by SDS-PAGE, despite the
lack of N- or O-glycosylation sites.
GENE FUNCTION
To determine whether NUCB2 binds Ca(2+) via its EF-hand domains, Kroll
et al. (1999) used heterologous overexpression of recombinant NUCB2
analogous to the mature protein and mutants with deletions in the
EF-hand domain in yeast. Experiments with the expression products
suggested that 1 mol of NUCB2 binds 2 mol of Ca(2+) ions. Fluorescence
titration exhibited 2 classes of Ca(2+)-binding sites with Kd values of
0.08 microM and 0.2 microM. Circular dichroism spectroscopy showed an
increase from 30% to 43% in the amount of alpha-helix in NUCB2 after
addition of calcium ions. Limited proteolytic digestion indicated a
Ca(2+)-dependent conformational change accompanied by an altered
accessibility to the enzyme.
Oh-I et al. (2006) demonstrated that the secreted protein nesfatin,
corresponding to NEFA/nucleobindin-2 (NUCB2), is expressed in the
appetite control hypothalamic nuclei in rats. Intracerebroventricular
injection of NUCB2 reduced feeding. Rat cerebrospinal fluid contains
nesfatin-1, an amino-terminal fragment derived from NUCB2, and its
expression is decreased in the hypothalamic paraventricular nucleus
under starved conditions. Intracerebroventricular injection of
nesfatin-1 decreased food intake in a dose-dependent manner, whereas
injection of an antibody neutralizing nesfatin-1 stimulated appetite. In
contrast, intracerebroventricular injection of other possible fragments
processed from NUCB2 did not promote satiety, and conversion of NUCB2 to
nesfatin-1 was necessary to induce feeding suppression. Chronic
intracerebroventricular injection of nesfatin-1 reduced body weight,
whereas rats gained body weight after chronic intracerebroventricular
injection of antisense morpholino oligonucleotide against the gene
encoding NUCB2. Nesfatin-1 induced anorexia occurs in Zucker rats with a
leptin receptor (601007) mutation, and an anti-nesfatin-1 antibody did
not block leptin (164160)-induced anorexia. In contrast, central
injection of alpha-melanocyte-stimulating hormone (176830) elevated
NUCB2 gene expression in the paraventricular nucleus, and satiety by
nesfatin-1 is abolished by an antagonist of the melanocortin-3/4
receptor (see 155540). Oh-I et al. (2006) concluded that nesfatin-1 is a
satiety molecule that is associated with melanocortin signaling in the
hypothalamus.
GENE STRUCTURE
By sequence analysis, Caldwell et al. (2001) determined that the NUCB2
gene contains at least 14 exons and spans approximately 50 kb.
MAPPING
By exon trapping and sequence analysis, DeAngelis et al. (1997)
identified the NUCB2 sequence on chromosome 11p15-p14.
*FIELD* RF
1. Barnikol-Watanabe, S.; Gross, N. A.; Gotz, H.; Henkel, T.; Karabinos,
A.; Kratzin, H.; Barnikol, H. U.; Hilschmann, N.: Human protein NEFA,
a novel DNA binding/EF-hand/leucine zipper protein: molecular cloning
and sequence analysis of the cDNA, isolation and characterization
of the protein. Biol. Chem. Hoppe Seyler 375: 497-512, 1994.
2. Caldwell, G. M.; Eddy, R. L.; Day, C. D.; Haley, L. H.; Cooper,
P. R.; Sait, S. S. J.; Hejtmancik, F.; Smith, R. J. H.; Morton, C.
C.; Higgins, M. J.; Shows, T. B.: Mapping of genes and transcribed
sequences in a gene rich 400-kb region on human chromosome 11p15.1-p14. Cytogenet.
Cell Genet. 92: 103-107, 2001.
3. DeAngelis, M.; Drury, S.; Doucet, J.; Sherry, S.; Buckley, L.;
Pelias, M.; Deininger, P.; Keats, B.; Batzer, M.: Construction of
a BAC contig and isolation of candidate genes in the Acadian Usher
syndrome (USH1C) critical region. (Abstract) Am. J. Hum. Genet. 61
(suppl.): A233 only, 1997.
4. Kroll, K. A.; Otte, S.; Hirschfeld, G.; Barnikol-Watanabe, S.;
Gotz, H.; Sternbach, H.; Kratzin, H. D.; Barnikol, H. U.; Hilschmann,
N.: Heterologous overexpression of human NEFA and studies on the
two EF-hand calcium-binding sites. Biochem. Biophys. Res. Commun. 260:
1-8, 1999.
5. Oh-I, S.; Shimizu, H.; Satoh, T.; Okada, S.; Adachi, S.; Inoue,
K.; Eguchi, H.; Yamamoto, M.; Imaki, T.; Hashimoto, K.; Tsuchiya,
T.; Monden, T.; Horiguchi, K.; Yamada, M.; Mori, M.: Identification
of nesfatin-1 as a satiety molecule in the hypothalamus. Nature 443:
709-712, 2006.
*FIELD* CN
Ada Hamosh - updated: 10/24/2006
*FIELD* CD
Carol A. Bocchini: 8/6/2003
*FIELD* ED
terry: 09/17/2010
alopez: 11/6/2006
terry: 10/24/2006
tkritzer: 8/8/2003
carol: 8/7/2003
tkritzer: 8/7/2003
carol: 8/6/2003
*RECORD*
*FIELD* NO
608020
*FIELD* TI
*608020 NUCLEOBINDIN 2; NUCB2
;;NEFA
*FIELD* TX
DESCRIPTION
Nucleobindin-2 is a calcium-binding EF-hand protein.
read more
CLONING
By screening cDNA libraries constructed from a human acute lymphoblastic
leukemia cell line with an anti-CALLA (120520) monoclonal antibody,
Barnikol-Watanabe et al. (1994) isolated a partial NUCB2 cDNA clone.
They assembled a full-length clone encoding a deduced 420-amino acid
protein, which they called NEFA, with a calculated molecular mass of 48
kD. The protein contains a basic amino acid-rich putative DNA-binding
domain with a potential nuclear targeting signal, 2 helix-loop-helix
motif regions, 2 concurrent EF-hand motifs, an acidic amino acid region
between the EF-hands, and a leucine zipper motif. The protein shares
high homology with human NUCB1 (601323). Isoelectric focusing
demonstrated the presence of NUCB2 on the plasma membrane, in the
cytosol, and in the culture supernatant. NUCB2 is a highly charged
protein with a relative molecular mass of 55 kD by SDS-PAGE, despite the
lack of N- or O-glycosylation sites.
GENE FUNCTION
To determine whether NUCB2 binds Ca(2+) via its EF-hand domains, Kroll
et al. (1999) used heterologous overexpression of recombinant NUCB2
analogous to the mature protein and mutants with deletions in the
EF-hand domain in yeast. Experiments with the expression products
suggested that 1 mol of NUCB2 binds 2 mol of Ca(2+) ions. Fluorescence
titration exhibited 2 classes of Ca(2+)-binding sites with Kd values of
0.08 microM and 0.2 microM. Circular dichroism spectroscopy showed an
increase from 30% to 43% in the amount of alpha-helix in NUCB2 after
addition of calcium ions. Limited proteolytic digestion indicated a
Ca(2+)-dependent conformational change accompanied by an altered
accessibility to the enzyme.
Oh-I et al. (2006) demonstrated that the secreted protein nesfatin,
corresponding to NEFA/nucleobindin-2 (NUCB2), is expressed in the
appetite control hypothalamic nuclei in rats. Intracerebroventricular
injection of NUCB2 reduced feeding. Rat cerebrospinal fluid contains
nesfatin-1, an amino-terminal fragment derived from NUCB2, and its
expression is decreased in the hypothalamic paraventricular nucleus
under starved conditions. Intracerebroventricular injection of
nesfatin-1 decreased food intake in a dose-dependent manner, whereas
injection of an antibody neutralizing nesfatin-1 stimulated appetite. In
contrast, intracerebroventricular injection of other possible fragments
processed from NUCB2 did not promote satiety, and conversion of NUCB2 to
nesfatin-1 was necessary to induce feeding suppression. Chronic
intracerebroventricular injection of nesfatin-1 reduced body weight,
whereas rats gained body weight after chronic intracerebroventricular
injection of antisense morpholino oligonucleotide against the gene
encoding NUCB2. Nesfatin-1 induced anorexia occurs in Zucker rats with a
leptin receptor (601007) mutation, and an anti-nesfatin-1 antibody did
not block leptin (164160)-induced anorexia. In contrast, central
injection of alpha-melanocyte-stimulating hormone (176830) elevated
NUCB2 gene expression in the paraventricular nucleus, and satiety by
nesfatin-1 is abolished by an antagonist of the melanocortin-3/4
receptor (see 155540). Oh-I et al. (2006) concluded that nesfatin-1 is a
satiety molecule that is associated with melanocortin signaling in the
hypothalamus.
GENE STRUCTURE
By sequence analysis, Caldwell et al. (2001) determined that the NUCB2
gene contains at least 14 exons and spans approximately 50 kb.
MAPPING
By exon trapping and sequence analysis, DeAngelis et al. (1997)
identified the NUCB2 sequence on chromosome 11p15-p14.
*FIELD* RF
1. Barnikol-Watanabe, S.; Gross, N. A.; Gotz, H.; Henkel, T.; Karabinos,
A.; Kratzin, H.; Barnikol, H. U.; Hilschmann, N.: Human protein NEFA,
a novel DNA binding/EF-hand/leucine zipper protein: molecular cloning
and sequence analysis of the cDNA, isolation and characterization
of the protein. Biol. Chem. Hoppe Seyler 375: 497-512, 1994.
2. Caldwell, G. M.; Eddy, R. L.; Day, C. D.; Haley, L. H.; Cooper,
P. R.; Sait, S. S. J.; Hejtmancik, F.; Smith, R. J. H.; Morton, C.
C.; Higgins, M. J.; Shows, T. B.: Mapping of genes and transcribed
sequences in a gene rich 400-kb region on human chromosome 11p15.1-p14. Cytogenet.
Cell Genet. 92: 103-107, 2001.
3. DeAngelis, M.; Drury, S.; Doucet, J.; Sherry, S.; Buckley, L.;
Pelias, M.; Deininger, P.; Keats, B.; Batzer, M.: Construction of
a BAC contig and isolation of candidate genes in the Acadian Usher
syndrome (USH1C) critical region. (Abstract) Am. J. Hum. Genet. 61
(suppl.): A233 only, 1997.
4. Kroll, K. A.; Otte, S.; Hirschfeld, G.; Barnikol-Watanabe, S.;
Gotz, H.; Sternbach, H.; Kratzin, H. D.; Barnikol, H. U.; Hilschmann,
N.: Heterologous overexpression of human NEFA and studies on the
two EF-hand calcium-binding sites. Biochem. Biophys. Res. Commun. 260:
1-8, 1999.
5. Oh-I, S.; Shimizu, H.; Satoh, T.; Okada, S.; Adachi, S.; Inoue,
K.; Eguchi, H.; Yamamoto, M.; Imaki, T.; Hashimoto, K.; Tsuchiya,
T.; Monden, T.; Horiguchi, K.; Yamada, M.; Mori, M.: Identification
of nesfatin-1 as a satiety molecule in the hypothalamus. Nature 443:
709-712, 2006.
*FIELD* CN
Ada Hamosh - updated: 10/24/2006
*FIELD* CD
Carol A. Bocchini: 8/6/2003
*FIELD* ED
terry: 09/17/2010
alopez: 11/6/2006
terry: 10/24/2006
tkritzer: 8/8/2003
carol: 8/7/2003
tkritzer: 8/7/2003
carol: 8/6/2003