ID   A0A7J7E4T4_DICBM        Unreviewed;       375 AA.
AC   A0A7J7E4T4;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   27-NOV-2024, entry version 6.
DE   RecName: Full=Endoplasmic reticulum junction formation protein lunapark {ECO:0000256|RuleBase:RU367073};
GN   ORFNames=HPG69_004788 {ECO:0000313|EMBL:KAF5910699.1};
OS   Diceros bicornis minor (South-central black rhinoceros).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Rhinocerotidae; Diceros.
OX   NCBI_TaxID=77932 {ECO:0000313|EMBL:KAF5910699.1, ECO:0000313|Proteomes:UP000551758};
RN   [1] {ECO:0000313|EMBL:KAF5910699.1, ECO:0000313|Proteomes:UP000551758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SBR-YM {ECO:0000313|EMBL:KAF5910699.1};
RC   TISSUE=Skin {ECO:0000313|EMBL:KAF5910699.1};
RX   PubMed=32585004;
RA   Moodley Y., Westbury M.V., Russo I.M., Gopalakrishnan S., Rakotoarivelo A.,
RA   Olsen R.A., Prost S., Tunstall T., Ryder O.A., Dalen L., Bruford M.W.;
RT   "Interspecific Gene Flow and the Evolution of Specialization in Black and
RT   White Rhinoceros.";
RL   Mol. Biol. Evol. 37:3105-3117(2020).
CC   -!- FUNCTION: Plays a role in determining ER morphology.
CC       {ECO:0000256|RuleBase:RU367073}.
CC   -!- SUBUNIT: Homodimer; homodimerization requires the C4-type zinc finger
CC       motif and decreases during mitosis in a phosphorylation-dependent
CC       manner. {ECO:0000256|ARBA:ARBA00047002, ECO:0000256|RuleBase:RU367073}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004215, ECO:0000256|RuleBase:RU367073}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004215,
CC       ECO:0000256|RuleBase:RU367073}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004215, ECO:0000256|RuleBase:RU367073}.
CC   -!- DOMAIN: The C4-type zinc finger motif is necessary both for its ER
CC       three-way tubular junction localization and formation.
CC       {ECO:0000256|RuleBase:RU367073}.
CC   -!- SIMILARITY: Belongs to the lunapark family.
CC       {ECO:0000256|ARBA:ARBA00009940, ECO:0000256|RuleBase:RU367073}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAF5910699.1}.
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DR   EMBL; JACDTQ010004070; KAF5910699.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7J7E4T4; -.
DR   Proteomes; UP000551758; Unassembled WGS sequence.
DR   GO; GO:0098826; C:endoplasmic reticulum tubular network membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0071788; P:endoplasmic reticulum tubular network maintenance; IEA:UniProtKB-UniRule.
DR   GO; GO:1903373; P:positive regulation of endoplasmic reticulum tubular network organization; IEA:UniProtKB-UniRule.
DR   InterPro; IPR040115; Lnp.
DR   InterPro; IPR019273; Lunapark_dom.
DR   PANTHER; PTHR22166; ENDOPLASMIC RETICULUM JUNCTION FORMATION PROTEIN LUNAPARK; 1.
DR   PANTHER; PTHR22166:SF12; ENDOPLASMIC RETICULUM JUNCTION FORMATION PROTEIN LUNAPARK; 1.
DR   Pfam; PF10058; zinc_ribbon_10; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU367073};
KW   Metal-binding {ECO:0000256|RuleBase:RU367073};
KW   Reference proteome {ECO:0000313|Proteomes:UP000551758};
KW   Zinc {ECO:0000256|RuleBase:RU367073};
KW   Zinc-finger {ECO:0000256|RuleBase:RU367073}.
FT   DOMAIN          201..250
FT                   /note="Lunapark"
FT                   /evidence="ECO:0000259|Pfam:PF10058"
FT   REGION          117..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..149
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..321
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   375 AA;  41463 MW;  2714B0133C807361 CRC64;
     MKTTFTDIHR IFDIDYLINA CHASKAKASP RAWLGPDLRS REEGRGLILS PGSVRQQTKP
     STVEVLENID KLEEVMEKET YKTAKLILER FDPDSKKAKS SIYFLFLFSE IRQRTAAQRN
     LSPTPTSSSQ GPPPQVPVSP GPPKDTSAPG GPPERTVTPV LSSNVLPRRL GSPATSVPGM
     GLHPPGPPLA RPILPRERGA LDRIVEYLVG DGPQNRYALI CQQCFSHNGM ALKEEFEYIA
     FRCAYCFFLN PARKTRPQAP RLPEFSFEKR QAVEDSSSVG HLPSGSAVSS ENQISEESLE
     EQDVLDNSTE QKDDKISDTE QTNQVIEKAS GTEEPEEKQE ETENEETLVK EAKSTVPRAD
     SIPDSELSGE SLMTV
//