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Database: UniProt
Entry: A0A3Q4GPI2_NEOBR
LinkDB: A0A3Q4GPI2_NEOBR
Original site: A0A3Q4GPI2_NEOBR 
ID   A0A3Q4GPI2_NEOBR        Unreviewed;      1133 AA.
AC   A0A3Q4GPI2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Sterol regulatory element-binding protein 1 {ECO:0000256|ARBA:ARBA00039749};
DE   AltName: Full=Sterol regulatory element-binding transcription factor 1 {ECO:0000256|ARBA:ARBA00042215};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000005292.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000005292.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBUNIT: Forms a tight complex with SCAP, the SCAP-SREBP complex, in
CC       the endoplasmic reticulum membrane. {ECO:0000256|ARBA:ARBA00038568}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC       membrane {ECO:0000256|ARBA:ARBA00004557}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004557}. Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SREBP family.
CC       {ECO:0000256|ARBA:ARBA00038460}.
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DR   AlphaFoldDB; A0A3Q4GPI2; -.
DR   STRING; 32507.ENSNBRP00000005292; -.
DR   Ensembl; ENSNBRT00000005449.1; ENSNBRP00000005292.1; ENSNBRG00000003534.1.
DR   GeneTree; ENSGT00940000159156; -.
DR   Proteomes; UP000261580; Unplaced.
DR   Bgee; ENSNBRG00000003534; Expressed in blood and 9 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   CDD; cd18921; bHLHzip_SREBP1; 1.
DR   Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   PANTHER; PTHR46062; STEROL REGULATORY ELEMENT-BINDING PROTEIN; 1.
DR   PANTHER; PTHR46062:SF2; STEROL REGULATORY ELEMENT-BINDING PROTEIN 1; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          362..412
FT                   /note="BHLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50888"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          974..996
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..474
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1133 AA;  121934 MW;  EB378E0FBD3535B5 CRC64;
     MNSLSFDDHS LDNLDPTLSL NDPSDIDTAL LSDIDDMLQL INNQDMEFGG LFDAPPYTTA
     PPMQEIHGLT QTITSASPPT TTTTPPSSSS ILSSNPHLDA LLGPPITRSS STPDKAFQPP
     TFQQSPLAQV PSSTQRQQPS SPQQAQSIRQ TQVEQPQPVL SPSAPSQAAS PNGSPGPNPA
     FSSTPQALFT SPAPQTPPQT QTQPQARTNY SSPNSYTAGS PSSVSTPATS LSSSPPSIQP
     VAIQAQLQGL TTASPLLTTS TSPPVQTVAA HVQQVPVLLQ PQFIKAESLL LTTLKPDPCM
     VTTVASPTSL ATTTPAQSTS LQAFMGGGTF LTTVPVMVDA EKLPINRIAI SGKPVGQPHK
     GEKRTAHNAI EKRYRSSIND KIMELKDLVA GTDAKLNKSA VLRKAIDYIR YLQQTNQKLK
     QENMALKMAA QKNKSLKDLV AMEVDGQADV KSELPTPPAS DVGSPTSFSH CGSDSEPDSP
     MGEDTKPNIG TPDQSTAGGS AVGMLDRSRM ALCTFTFLFL SLNPLAALFC SSGSSSSGNT
     EAVSTHHAGR TVLGVDVAGD SWGWMDWMLP TILVWLLNGI LVSGVLIRLL VYGEPVTRPH
     SGSSVLFWRH RKQADLDLAR GDFAQASHNL WTCLKALGRP LPTSQLDLAC AALWSLLRFC
     LQRLWVGRWL AARAGGLRSD RPLQEDACKS SRDAALVYHR LHQLHMTGKL NGSHLSAVHM
     SLSAVNLAEC SGSCLPVASL AEIYVSAALR VKASLPRVLH FTSRVFLSSA RQACLSSSGS
     VPPAMQWLCH PLGHRFFVDG DWAIRSTPKE SIYSQAGNTV DPLAQVTQAF REHLLEKALY
     CVAQPRGEKN TSCDPHSKWW SSITVVIINW LQGDDAAAER LYPTVEHLPR SLQNAESLLP
     KACLNTFRAV RALLSKPENC QLSLSYSDKA SALLRDSLNL GPHCHSSSLD KVVQLLLCDL
     LLVMRTNVWR LQQQGATPTG QGSAGTSGPA GIQQASPPEL VGFQQDLSSL RKLAQSFRPA
     MRRLFLHEAT ARLMAGASPT RTHQLLDRSL RRRATPGAKT EECEMRPGQR EQAEAVMLAC
     RYLPPSFLSA PGQRVGMLAD AARTLEKLGD KRTLHDCQQM IIKLGSGTTV TNS
//
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