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Database: UniProt
Entry: A0A401S2S8_CHIPU
LinkDB: A0A401S2S8_CHIPU
Original site: A0A401S2S8_CHIPU 
ID   A0A401S2S8_CHIPU        Unreviewed;       340 AA.
AC   A0A401S2S8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=3CxxC-type domain-containing protein {ECO:0000259|SMART:SM01328};
GN   ORFNames=chiPu_0003086 {ECO:0000313|EMBL:GCC24684.1};
OS   Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC   Chiloscyllium.
OX   NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC24684.1, ECO:0000313|Proteomes:UP000287033};
RN   [1] {ECO:0000313|EMBL:GCC24684.1, ECO:0000313|Proteomes:UP000287033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA   Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA   Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA   Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA   Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT   "Shark genomes provide insights into elasmobranch evolution and the origin
RT   of vertebrates.";
RL   Nat. Ecol. Evol. 2:1761-1771(2018).
CC   -!- SIMILARITY: Belongs to the ZAR1 family.
CC       {ECO:0000256|ARBA:ARBA00034699}.
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:GCC24684.1}.
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DR   EMBL; BEZZ01000064; GCC24684.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401S2S8; -.
DR   OMA; RVCEKSY; -.
DR   Proteomes; UP000287033; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IEA:UniProt.
DR   GO; GO:0017148; P:negative regulation of translation; IEA:UniProt.
DR   GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR026775; Zar1.
DR   InterPro; IPR027377; ZAR1/RTP1-5-like_Znf-3CxxC.
DR   PANTHER; PTHR31054:SF6; ZYGOTE ARREST PROTEIN 1; 1.
DR   PANTHER; PTHR31054; ZYGOTE ARREST PROTEIN 1-LIKE ISOFORM X1; 1.
DR   Pfam; PF13695; zf-3CxxC; 1.
DR   SMART; SM01328; zf-3CxxC; 1.
PE   3: Inferred from homology;
KW   Differentiation {ECO:0000256|ARBA:ARBA00022943};
KW   Oogenesis {ECO:0000256|ARBA:ARBA00022943};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287033}.
FT   DOMAIN          241..326
FT                   /note="3CxxC-type"
FT                   /evidence="ECO:0000259|SMART:SM01328"
FT   REGION          105..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   340 AA;  38723 MW;  52432CD9C1A45CD9 CRC64;
     MATLGEDAFD YIYSPYNPYS YQYLSSRPKA SSWRPRGYLN NYGDPGEYFD NYQRAQLKAI
     LSQVNPNLTP RVRKANTKDV GVQVNPKIDA SVQCSLGPRT LLTMTMRPRR RPSQTQVQGS
     PASMPRNVRF RRTMAIYSPI VSPNLNSFVY RGEPRQAARE TAGKPEQQEE GEPEAVKQEE
     PAPEQDLRAG EKGGEPADSP ALPAGELSET PAENGNKPEA ADTVPKTGTS EKRLRFQFLE
     QKYGYFHCKD CSARWESAYV WCVQGTNKVY FKQFCRTCEK AYNPYRVEDI TCQTCKQTRC
     TCPVKMRHVD PKRPHRQDLC GRCKGKRLSC DSTFSFKYII
//
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