ID   BRNP1_HUMAN             Reviewed;         761 AA.
AC   O60477; Q6IPV6; Q6P1A0; Q8WU22;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   13-FEB-2019, entry version 135.
DE   RecName: Full=BMP/retinoic acid-inducible neural-specific protein 1;
DE   AltName: Full=Deleted in bladder cancer protein 1;
DE   Flags: Precursor;
GN   Name=BRINP1; Synonyms=DBC1, DBCCR1, FAM5A; ORFNames=IB3089A;
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), VARIANT THR-437, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=9545632; DOI=10.1006/geno.1997.5165;
RA   Habuchi T., Luscombe M., Elder P.A., Knowles M.A.;
RT   "Structure and methylation-based silencing of a gene (DBCCR1) within a
RT   candidate bladder cancer tumor suppressor region at 9q32-q33.";
RL   Genomics 48:277-288(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Brain, and Kidney;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND VARIANTS ARG-347; HIS-358 AND
RP   THR-437.
RX   PubMed=11420708; DOI=10.1038/sj.onc.1204432;
RA   Nishiyama H., Gill J.H., Pitt E., Kennedy W., Knowles M.A.;
RT   "Negative regulation of G(1)/S transition by the candidate bladder
RT   tumour suppressor gene DBCCR1.";
RL   Oncogene 20:2956-2964(2001).
RN   [5]
RP   FUNCTION.
RX   PubMed=14712213; DOI=10.1038/sj.onc.1206642;
RA   Wright K.O., Messing E.M., Reeder J.E.;
RT   "DBCCR1 mediates death in cultured bladder tumor cells.";
RL   Oncogene 23:82-90(2004).
RN   [6]
RP   FUNCTION.
RX   PubMed=16369496; DOI=10.1038/sj.onc.1209228;
RA   Louhelainen J.P., Hurst C.D., Pitt E., Nishiyama H., Pickett H.A.,
RA   Knowles M.A.;
RT   "DBC1 re-expression alters the expression of multiple components of
RT   the plasminogen pathway.";
RL   Oncogene 25:2409-2419(2006).
RN   [7]
RP   VARIANT [LARGE SCALE ANALYSIS] THR-712.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Inhibits cell proliferation by negative regulation of
CC       the G1/S transition. Mediates cell death which is not of the
CC       classical apoptotic type and regulates expression of components of
CC       the plasminogen pathway. {ECO:0000269|PubMed:11420708,
CC       ECO:0000269|PubMed:14712213, ECO:0000269|PubMed:16369496}.
CC   -!- INTERACTION:
CC       Q5BKZ1:ZNF326; NbExp=5; IntAct=EBI-3904864, EBI-2560158;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11420708}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O60477-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O60477-2; Sequence=VSP_017022, VSP_017023;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=O60477-3; Sequence=VSP_017021;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain. Weakly expressed in
CC       heart, lung, skeletal muscle, kidney, thymus, prostate, testis and
CC       small intestine. {ECO:0000269|PubMed:9545632}.
CC   -!- MISCELLANEOUS: Silenced by methylation in 50% of bladder cancer
CC       cell lines.
CC   -!- SIMILARITY: Belongs to the BRINP family. {ECO:0000305}.
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; AF027734; AAC39691.1; -; mRNA.
DR   EMBL; AL138894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL353773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC021560; AAH21560.1; -; mRNA.
DR   EMBL; BC065196; AAH65196.1; -; mRNA.
DR   EMBL; BC071702; AAH71702.1; -; mRNA.
DR   CCDS; CCDS6822.1; -. [O60477-1]
DR   PIR; T09052; T09052.
DR   RefSeq; NP_055433.2; NM_014618.2. [O60477-1]
DR   UniGene; Hs.532316; -.
DR   ProteinModelPortal; O60477; -.
DR   BioGrid; 107988; 31.
DR   IntAct; O60477; 22.
DR   STRING; 9606.ENSP00000265922; -.
DR   TCDB; 1.C.39.17.1; the membrane attack complex/perforin (macpf) family.
DR   iPTMnet; O60477; -.
DR   PhosphoSitePlus; O60477; -.
DR   BioMuta; BRINP1; -.
DR   PaxDb; O60477; -.
DR   PeptideAtlas; O60477; -.
DR   PRIDE; O60477; -.
DR   ProteomicsDB; 49417; -.
DR   ProteomicsDB; 49418; -. [O60477-2]
DR   ProteomicsDB; 49419; -. [O60477-3]
DR   Ensembl; ENST00000265922; ENSP00000265922; ENSG00000078725. [O60477-1]
DR   Ensembl; ENST00000373964; ENSP00000363075; ENSG00000078725. [O60477-2]
DR   GeneID; 1620; -.
DR   KEGG; hsa:1620; -.
DR   UCSC; uc004bkc.3; human. [O60477-1]
DR   CTD; 1620; -.
DR   DisGeNET; 1620; -.
DR   EuPathDB; HostDB:ENSG00000078725.12; -.
DR   GeneCards; BRINP1; -.
DR   H-InvDB; HIX0034750; -.
DR   HGNC; HGNC:2687; BRINP1.
DR   HPA; HPA038828; -.
DR   MIM; 602865; gene.
DR   neXtProt; NX_O60477; -.
DR   OpenTargets; ENSG00000078725; -.
DR   PharmGKB; PA27156; -.
DR   eggNOG; ENOG410IF4X; Eukaryota.
DR   eggNOG; ENOG410XQ74; LUCA.
DR   GeneTree; ENSGT00940000158084; -.
DR   HOGENOM; HOG000049122; -.
DR   HOVERGEN; HBG081412; -.
DR   InParanoid; O60477; -.
DR   OMA; RTCVCHT; -.
DR   OrthoDB; 157712at2759; -.
DR   PhylomeDB; O60477; -.
DR   TreeFam; TF331600; -.
DR   GeneWiki; DBC1; -.
DR   GenomeRNAi; 1620; -.
DR   PRO; PR:O60477; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   Bgee; ENSG00000078725; Expressed in 140 organ(s), highest expression level in primary visual cortex.
DR   Genevisible; O60477; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR   GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
DR   GO; GO:0007050; P:cell cycle arrest; IEA:UniProtKB-KW.
DR   GO; GO:0008219; P:cell death; IDA:UniProtKB.
DR   GO; GO:0071300; P:cellular response to retinoic acid; IBA:GO_Central.
DR   GO; GO:0035640; P:exploration behavior; IEA:Ensembl.
DR   GO; GO:0042711; P:maternal behavior; IEA:Ensembl.
DR   GO; GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB.
DR   GO; GO:0045930; P:negative regulation of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; IEA:Ensembl.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IBA:GO_Central.
DR   GO; GO:0007614; P:short-term memory; IEA:Ensembl.
DR   GO; GO:0035176; P:social behavior; IEA:Ensembl.
DR   GO; GO:0071625; P:vocalization behavior; IEA:Ensembl.
DR   InterPro; IPR033237; BRINP.
DR   InterPro; IPR020864; MACPF.
DR   PANTHER; PTHR15564; PTHR15564; 1.
DR   Pfam; PF01823; MACPF; 1.
DR   SMART; SM00457; MACPF; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Complete proteome; Cytoplasm;
KW   Glycoprotein; Growth arrest; Polymorphism; Reference proteome; Signal.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    761       BMP/retinoic acid-inducible neural-
FT                                specific protein 1.
FT                                /FTId=PRO_0000045766.
FT   DOMAIN       68    251       MACPF.
FT   CARBOHYD    156    156       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    433    433       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    443    443       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    553    553       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    599    599       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    631    631       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    677    677       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VAR_SEQ       1    285       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_017021.
FT   VAR_SEQ     308    320       DEFKSFMKRLPSN -> GRESHSVPLHEWP (in
FT                                isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_017022.
FT   VAR_SEQ     321    761       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_017023.
FT   VARIANT     347    347       S -> R (common polymorphism).
FT                                {ECO:0000269|PubMed:11420708}.
FT                                /FTId=VAR_029989.
FT   VARIANT     358    358       R -> H (common polymorphism;
FT                                dbSNP:rs17476783).
FT                                {ECO:0000269|PubMed:11420708}.
FT                                /FTId=VAR_029990.
FT   VARIANT     437    437       A -> T (in dbSNP:rs1043377).
FT                                {ECO:0000269|PubMed:11420708,
FT                                ECO:0000269|PubMed:9545632}.
FT                                /FTId=VAR_024930.
FT   VARIANT     712    712       P -> T (in a colorectal cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036336.
SQ   SEQUENCE   761 AA;  88760 MW;  16FF47082FD52252 CRC64;
     MNWRFVELLY FLFIWGRISV QPSHQEPAGT DQHVSKEFDW LISDRGPFHH SRSYLSFVER
     HRQGFTTRYK IYREFARWKV RNTAIERRDL VRHPVPLMPE FQRSIRLLGR RPTTQQFIDT
     IIKKYGTHLL ISATLGGEEA LTMYMDKSRL DRKSGNATQS VEALHQLASS YFVDRDGTMR
     RLHEIQISTG AIKVTETRTG PLGCNSYDNL DSVSSVLLQS TESKLHLQGL QIIFPQYLQE
     KFVQSALSYI MCNGEGEYLC QNSQCRCQCA EEFPQCNCPI TDIQIMEYTL ANMAKSWAEA
     YKDLENSDEF KSFMKRLPSN HFLTIGSIHQ HWGNDWDLQN RYKLLQSATE AQRQKIQRTA
     RKLFGLSVRC RHNPNHQLPR ERTIQQWLAR VQSLLYCNEN GFWGTFLESQ RSCVCHGSTT
     LCQRPIPCVI GGNNSCAMCS LANISLCGSC NKGYKLYRGR CEPQNVDSER SEQFISFETD
     LDFQDLELKY LLQKMDSRLY VHTTFISNEI RLDTFFDPRW RKRMSLTLKS NKNRMDFIHM
     VIGMSMRICQ MRNSSLDPMF FVYVNPFSGS HSEGWNMPFG EFGYPRWEKI RLQNSQCYNW
     TLLLGNRWKT FFETVHIYLR SRTRLPTLLR NETGQGPVDL SDPSKRQFYI KISDVQVFGY
     SLRFNADLLR SAVQQVNQSY TQGGQFYSSS SVMLLLLDIR DRINRLAPPV APGKPQLDLF
     SCMLKHRLKL TNSEIIRVNH ALDLYNTEIL KQSDQMTAKL C
//