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BRNP2_PONAB
ID   BRNP2_PONAB             Reviewed;         783 AA.
AC   Q5RDR5;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=BMP/retinoic acid-inducible neural-specific protein 2;
DE   Flags: Precursor;
GN   Name=BRINP2; Synonyms=FAM5B;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inhibits neuronal cell proliferation by negative regulation
CC       of the cell cycle transition. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the BRINP family. {ECO:0000305}.
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DR   EMBL; CR857837; CAH90092.1; -; mRNA.
DR   AlphaFoldDB; Q5RDR5; -.
DR   STRING; 9601.ENSPPYP00000000550; -.
DR   eggNOG; ENOG502QQZS; Eukaryota.
DR   InParanoid; Q5RDR5; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0045930; P:negative regulation of mitotic cell cycle; IEA:InterPro.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:InterPro.
DR   InterPro; IPR033237; BRINP.
DR   InterPro; IPR020864; MACPF.
DR   PANTHER; PTHR15564; PTHR15564; 1.
DR   Pfam; PF19052; BRINP; 1.
DR   Pfam; PF01823; MACPF; 1.
DR   SMART; SM00457; MACPF; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Glycoprotein; Growth arrest; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..783
FT                   /note="BMP/retinoic acid-inducible neural-specific protein
FT                   2"
FT                   /id="PRO_0000045772"
FT   DOMAIN          85..281
FT                   /note="MACPF"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        354
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        473
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        579
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        626
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        658
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   783 AA;  88975 MW;  654A033832DF2184 CRC64;
     MRWQCGTRFR GLRPVVAPWT ALLALGLPGW VLAVSATAAA VVPEQHASTA GQHPLDWLLT
     DRGPFHRAQE YADFMERYRQ GFTTRYRIYR EFARWKVNNL ALERKDFFSL PLPLAPESIR
     NIRLLGRRPN LQQVTENLIK KYGTHFLLSA TLGGEESLTI FVDKRKLGRK TETTGGASII
     GGSGNSTAVS LETLHQLAAS YFIDRESTLR RLHHIQIATG AIKVTETRTG PLGCSNYDNL
     DSVSSVLVQS PENKVQLLGL QVLLPEYLRE RFVAAALSYI TCSSEGELVC KENDCWCKCS
     PTFPDCNCPD ADIQAMEDSL LQIQDSWATH NRQFEESEEF QALLKRLPDD RFLNSTAISQ
     FWAMDTSLQH RYQQLGAGLK VLFKKTHRIV RRLFNLCKRC HRQPRFRLPK ERSLSYWWNR
     IQSLLYCGES TFPGTFLEQS HSCTCPYDQS SCQGPIPCAL GEGPACAHCA PDNSTRCGSC
     NPGYVLAQGL CRPEVAESLE NFLGLETDLQ DLELKYLLQK QDSRIEVHSI FISNDMRLGS
     WFDPSWRKRM LLTLKSNKYK PGLVHVMLAL SLQICLTKNS TLEPVMAIYV NPFGGSHSES
     WFMPVNEGSF PDWERTNVDA AAQCQNWTIT LGNRWKTFFE TVHVYLRSRI KSLDDSSNET
     IYYEPLEMTD PSKNLGYMKI NTLQVFGYSL PFDPDAIRDL ILQLDYPYTQ GSQDSALLQL
     IELRDRVNQL SPPGKVRLDL FSCLLRHRLK LANNEVGRIQ SSLRAFNSKL PNPVEYETGK
     LCS
 
 
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