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Database: UniProt
Entry: A0AAD7TCQ1_9TELE
LinkDB: A0AAD7TCQ1_9TELE
Original site: A0AAD7TCQ1_9TELE 
ID   A0AAD7TCQ1_9TELE        Unreviewed;       670 AA.
AC   A0AAD7TCQ1;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   28-JAN-2026, entry version 7.
DE   RecName: Full=Suppressor of cytokine signaling 5 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AAFF_G00142100 {ECO:0000313|EMBL:KAJ8418501.1};
OS   Aldrovandia affinis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Notacanthiformes; Halosauridae;
OC   Aldrovandia.
OX   NCBI_TaxID=143900 {ECO:0000313|EMBL:KAJ8418501.1, ECO:0000313|Proteomes:UP001221898};
RN   [1] {ECO:0000313|EMBL:KAJ8418501.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NC1722 {ECO:0000313|EMBL:KAJ8418501.1};
RX   PubMed=36758078;
RA   Parey E., Louis A., Montfort J., Bouchez O., Roques C., Iampietro C.,
RA   Lluch J., Castinel A., Donnadieu C., Desvignes T., Floi Bucao C.,
RA   Jouanno E., Wen M., Mejri S., Dirks R., Jansen H., Henkel C., Chen W.J.,
RA   Zahm M., Cabau C., Klopp C., Thompson A.W., Robinson-Rechavi M.,
RA   Braasch I., Lecointre G., Bobe J., Postlethwait J.H., Berthelot C.,
RA   Roest Crollius H., Guiguen Y.;
RT   "Genome structures resolve the early diversification of teleost fishes.";
RL   Science 379:572-575(2023).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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:KAJ8418501.1}.
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DR   EMBL; JAINUG010000002; KAJ8418501.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AAD7TCQ1; -.
DR   Proteomes; UP001221898; Unassembled WGS sequence.
DR   GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IEA:TreeGrafter.
DR   GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IEA:TreeGrafter.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:TreeGrafter.
DR   FunFam; 3.30.505.10:FF:000028; Suppressor of cytokine signaling 5; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR022252; SOCS4/SOCS5_dom.
DR   InterPro; IPR001496; SOCS_box.
DR   InterPro; IPR036036; SOCS_box-like_dom_sf.
DR   PANTHER; PTHR10155; PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR10155:SF15; SUPPRESSOR OF CYTOKINE SIGNALING 5; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF12610; SOCS; 1.
DR   Pfam; PF07525; SOCS_box; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00253; SOCS; 1.
DR   SMART; SM00969; SOCS_box; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF158235; SOCS box-like; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50225; SOCS; 1.
PE   4: Predicted;
KW   Growth regulation {ECO:0000256|ARBA:ARBA00022604};
KW   Reference proteome {ECO:0000313|Proteomes:UP001221898};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191};
KW   Signal transduction inhibitor {ECO:0000256|ARBA:ARBA00022700};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          515..610
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          605..654
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000259|PROSITE:PS50225"
FT   REGION          266..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          393..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..283
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..429
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..486
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   670 AA;  73695 MW;  76A8110BFF5702AA CRC64;
     MASGNAARDP AFSVEVKKVK GADSQIPPPI GINGQEFRTI AVDFIALFNM ASELAVREER
     VKRLVASVGP RLSSFVAGQP SGAGGAVRGG ASYLDCSPAQ TRFEVVPSSV WLPGSQRRRR
     RSRFLSWPTP AVGPAPGSSR NLCFLFMHYR TPQCYNFASL MVSDPRSMEK VGKMWNNLKS
     RCQTLFHPET PGAGEGRLEV SGVRCLVDPG RGMRLGEPLG SRAGSPARSV SPLPLVVAAD
     GLQGPARRGH NCVSDIPQIV EITIDRESGG GGDSAARGPG GGTPLARRDS YSRHAPWGAK
     KKHSRYGVSS VHDMDPCGGR GPGSRSLRQR IHDTVGLCLP LRPRPPRGAS SKTAALFASK
     RKIHLTELML ETCPFPPGSD LAHKWHLIKQ HTAPVSPQSS GTLLDAFDPA RPSPEDEEER
     LRERRRLSIE EGVDPPPNAQ IHTFEATAQP VDCDSEEDST TLCLQSRRPK QRHASGGGGD
     SGGHAGRQGP WKVHTQIDYI HCLVPDLLHI TGLPCYWGVM DRYEAEALLE GRPEGTFLLR
     DSAQEDYLFS VSFRRYNRSL HARIEQWNHN FSFDAHDPCV FHASTVTGLL EHYKDPGSCM
     FFEPLLTAPL HRTFPFGLQH LARAAICRRT TYDGIGGLPL PPALQDFLKE YHYKQKVRVR
     WLEREPLKIK
//
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