NBL1_RAT
ID NBL1_RAT Reviewed; 178 AA.
AC Q06880; Q6P750;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Neuroblastoma suppressor of tumorigenicity 1;
DE AltName: Full=N03;
DE AltName: Full=Zinc finger protein DAN;
DE Flags: Precursor;
GN Name=Nbl1; Synonyms=Dan;
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].
RX PubMed=8385338; DOI=10.1073/pnas.90.7.2593;
RA Ozaki T., Sakiyama S.;
RT "Molecular cloning and characterization of a cDNA showing negative
RT regulation in v-src-transformed 3Y1 rat fibroblasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2593-2597(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7942277; DOI=10.1016/0065-2571(94)90019-1;
RA Sakiyama S., Ozaki T., Enomoto H.;
RT "Molecular cloning and characterization of a cDNA showing tumor-suppressive
RT activity in V-SRC-transformed 3Y1 rat fibroblasts.";
RL Adv. Enzyme Regul. 34:247-255(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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).
CC -!- FUNCTION: Possible candidate as a tumor suppressor gene of
CC neuroblastoma. May play an important role in preventing cells from
CC entering the final stage (G1/S) of the transformation process.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Most abundant in lung, brain, intestine and kidney.
CC -!- SIMILARITY: Belongs to the DAN family. {ECO:0000305}.
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DR EMBL; X66872; CAA47344.1; -; mRNA.
DR EMBL; S72637; AAB32215.1; -; mRNA.
DR EMBL; BC061833; AAH61833.1; -; mRNA.
DR PIR; A47291; A47291.
DR RefSeq; NP_113797.1; NM_031609.1.
DR AlphaFoldDB; Q06880; -.
DR SMR; Q06880; -.
DR BioGRID; 248400; 1.
DR IntAct; Q06880; 1.
DR STRING; 10116.ENSRNOP00000064345; -.
DR PhosphoSitePlus; Q06880; -.
DR PaxDb; Q06880; -.
DR GeneID; 50594; -.
DR KEGG; rno:50594; -.
DR CTD; 4681; -.
DR RGD; 3151; Nbl1.
DR eggNOG; ENOG502RYP0; Eukaryota.
DR InParanoid; Q06880; -.
DR OrthoDB; 1517793at2759; -.
DR PhylomeDB; Q06880; -.
DR PRO; PR:Q06880; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0036122; F:BMP binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0016015; F:morphogen activity; ISO:RGD.
DR GO; GO:0048018; F:receptor ligand activity; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0048263; P:determination of dorsal identity; ISO:RGD.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0090027; P:negative regulation of monocyte chemotaxis; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; ISO:RGD.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISO:RGD.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:RGD.
DR GO; GO:0038098; P:sequestering of BMP from receptor via BMP binding; ISO:RGD.
DR GO; GO:0035582; P:sequestering of BMP in extracellular matrix; ISO:RGD.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR004133; DAN.
DR InterPro; IPR016728; Neuroblast_suppress_tumour_1.
DR Pfam; PF03045; DAN; 1.
DR PIRSF; PIRSF018557; DAN_sub; 1.
DR SMART; SM00041; CT; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Reference proteome; Secreted; Signal; Tumor suppressor.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..178
FT /note="Neuroblastoma suppressor of tumorigenicity 1"
FT /id="PRO_0000006724"
FT DOMAIN 34..123
FT /note="CTCK"
FT REGION 130..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 34..84
FT /evidence="ECO:0000250"
FT DISULFID 48..98
FT /evidence="ECO:0000250"
FT DISULFID 58..117
FT /evidence="ECO:0000250"
FT DISULFID 62..119
FT /evidence="ECO:0000250"
FT DISULFID 81..122
FT /evidence="ECO:0000255"
FT CONFLICT 157
FT /note="C -> G (in Ref. 3; AAH61833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 178 AA; 19191 MW; 4786AF6DC3510212 CRC64;
MLWVLVGTVL PVMLLAAPPP INKLALFPDK SAWCEAKNIT QIVGHSGCEA KSIQNRACLG
QCFSYSVPNT FPQSTESLVH CDSCMPAQSM WEIVTLECPG HEEVPRVDKL VEKIVHCSCQ
ACGKEPSHEG LNVYMQGEDG PGSQPGSHSH SHPHPGCQTP EPEEPPGAPQ VEEEGAED