ID   A0A3Q1FJW1_9TELE        Unreviewed;       912 AA.
AC   A0A3Q1FJW1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Caprin-2-like {ECO:0000313|Ensembl:ENSAPOP00000016699.1};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000016699.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000016699.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the caprin family.
CC       {ECO:0000256|ARBA:ARBA00007950}.
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   AlphaFoldDB; A0A3Q1FJW1; -.
DR   STRING; 80966.ENSAPOP00000016699; -.
DR   Ensembl; ENSAPOT00000025756.1; ENSAPOP00000016699.1; ENSAPOG00000019808.1.
DR   GeneTree; ENSGT00940000153438; -.
DR   InParanoid; A0A3Q1FJW1; -.
DR   OrthoDB; 5403347at2759; -.
DR   Proteomes; UP000257200; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0009950; P:dorsal/ventral axis specification; IEA:Ensembl.
DR   GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR   Gene3D; 2.60.120.40; -; 1.
DR   InterPro; IPR001073; C1q_dom.
DR   InterPro; IPR028816; Caprin.
DR   InterPro; IPR022070; Caprin-1_C.
DR   InterPro; IPR041637; Caprin-1_dimer.
DR   InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR   PANTHER; PTHR22922:SF5; CAPRIN-2; 1.
DR   PANTHER; PTHR22922; GPI-ANCHORED PROTEIN P137; 1.
DR   Pfam; PF00386; C1q; 1.
DR   Pfam; PF12287; Caprin-1_C; 1.
DR   Pfam; PF18293; Caprin-1_dimer; 1.
DR   PRINTS; PR00007; COMPLEMNTC1Q.
DR   SMART; SM00110; C1Q; 1.
DR   SUPFAM; SSF49842; TNF-like; 1.
DR   PROSITE; PS50871; C1Q; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW   Protein synthesis inhibitor {ECO:0000256|ARBA:ARBA00023193};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          778..912
FT                   /note="C1q"
FT                   /evidence="ECO:0000259|PROSITE:PS50871"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          414..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          684..741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          111..138
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        349..364
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..561
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        717..741
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   912 AA;  101195 MW;  17C0A54BCE4E84AB CRC64;
     MVQLSPSPTP DVSPPPEHSV EEEEEVLEDP KVGLPDGSLQ LSLEVSTTYH GYETYIEDGL
     ICLKHKIRNL EKKKLKLRDY KKRLNRGEVL NKDQMVAVEK YDEVVHNLEF ARELHKTLDG
     LTQNLLRAQK KEQMLKVEAE RRRLTTVLQV QHLLTCLQQD HIRKDLLAGR NKAPHIPAQR
     LHSLSQLAVL LGVQRDNTLS LEKQMEQASL VYLDLLEGKD KPVAGSTFKL LKEELTMLLN
     CKFFSCLPSP PSKTPEGMLS SSSHNTVLKS KPNEVSKEFL NRLYLTDMET PPTLSWKEDF
     QALRDREPPD CWDMESPDRP SSLQAAVHKP WRGAATFIPK VVPVSSKKQS DCKQRKERKA
     KGEQNANLAV HVDMPVEIFN SPSAFPKDPI LRKQHLEDLM TKIHGSFTFM QDSLLDGESS
     PTNDHSRLKR SPSGSPSPIS QTYLRSPPDV LPKTMHSTPL PARLMECKAS LNGSDQSLET
     CDQELSSKDL PDEPLQLAER KTFPSPPVYR RESTISINLE ENNSPQTPVN DSGKPSPSNG
     SASCASTPPQ GQSFSTPPTR KTLTSTQFQN IQTVFKATAT LNHNEEPNYK ADPAAFSEPM
     YSTASTQTPP EFAPAEDELQ SVYQTDYTLG NGGQIFLSPG QSGGGGSRAS HSYNTRGVVR
     GMARGGRGLA QSFRTSGWHR GGSCIPQVHL RDSGPLPYSA RDSGYQHSYR RGGGRHNSSA
     AWSSSAQVGS PDQDGTCTLV DSGQGDLLSV STMEVPLTPH GHPHHPPALL PMPLYSPPHS
     LRVAFTASRT ANFAPGNLDQ PIVFDQLHSN LGEMYDIHIG RFTCPVNGTY VFTFHILKLA
     VNVPLYINLM RNEEVMVSAY ANDGAPDHET ASNHAILPLF QGDQVWLRLH RGAIYGSTWK
     YSTFSGFLLY QD
//