ID S9XDI8_CAMFR Unreviewed; 657 AA.
AC S9XDI8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Gamma-interferon-inducible lysosomal thiol reductase {ECO:0000256|RuleBase:RU369109};
DE EC=1.8.-.- {ECO:0000256|RuleBase:RU369109};
DE AltName: Full=Gamma-interferon-inducible protein IP-30 {ECO:0000256|RuleBase:RU369109};
GN ORFNames=CB1_000172059 {ECO:0000313|EMBL:EPY88487.1};
OS Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY88487.1, ECO:0000313|Proteomes:UP000030684};
RN [1] {ECO:0000313|EMBL:EPY88487.1, ECO:0000313|Proteomes:UP000030684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684};
RX PubMed=23149746;
RG Bactrian Camels Genome Sequencing and Analysis Consortium;
RA Jirimutu, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., Wang L.,
RA Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., Zhang W.,
RA Batmunkh M., Ts B., Narenbatu, Unierhu, Bat-Ireedui S., Gao H.,
RA Baysgalan B., Li Q., Jia Z., Turigenbayila, Subudenggerile, Narenmanduhu,
RA Wang Z., Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt, Erdemt, Altansha,
RA Altansukh, Liu T., Cao M., Aruuntsever, Bayart, Hosblig, He F., Zha-ti A.,
RA Zheng G., Qiu F., Sun Z., Zhao L., Zhao W., Liu B., Li C., Chen Y.,
RA Tang X., Guo C., Liu W., Ming L., Temuulen, Cui A., Li Y., Gao J., Li J.,
RA Wurentaodi, Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T.,
RA Bayaer T., Li Y., Meng H.;
RT "Genome sequences of wild and domestic bactrian camels.";
RL Nat. Commun. 3:1202-1202(2012).
CC -!- FUNCTION: Lysosomal thiol reductase that can reduce protein disulfide
CC bonds. Facilitates the complete unfolding of proteins destined for
CC lysosomal degradation. Plays an important role in antigen processing.
CC {ECO:0000256|RuleBase:RU369109}.
CC -!- SUBUNIT: Dimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00011615,
CC ECO:0000256|RuleBase:RU369109}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU369109}.
CC Lysosome {ECO:0000256|RuleBase:RU369109}.
CC -!- SIMILARITY: Belongs to the GILT family. {ECO:0000256|ARBA:ARBA00005679,
CC ECO:0000256|RuleBase:RU369109}.
CC -!- SIMILARITY: Belongs to the PI3K p85 subunit family.
CC {ECO:0000256|ARBA:ARBA00009442}.
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DR EMBL; KB016467; EPY88487.1; -; Genomic_DNA.
DR AlphaFoldDB; S9XDI8; -.
DR Proteomes; UP000030684; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd12926; iSH2_PIK3R2; 1.
DR CDD; cd09930; SH2_cSH2_p85_like; 1.
DR CDD; cd09942; SH2_nSH2_p85_like; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR InterPro; IPR004911; Interferon-induced_GILT.
DR InterPro; IPR032498; PI3K_P85_iSH2.
DR InterPro; IPR035020; PI3kinase_P85_cSH2.
DR InterPro; IPR035022; PI3kinase_P85_nSH2.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR PANTHER; PTHR10155; PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR10155:SF10; PI3K21B, ISOFORM B; 1.
DR Pfam; PF03227; GILT; 1.
DR Pfam; PF16454; PI3K_P85_iSH2; 1.
DR Pfam; PF00017; SH2; 2.
DR PRINTS; PR00678; PI3KINASEP85.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00252; SH2; 2.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR PROSITE; PS50001; SH2; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|RuleBase:RU369109};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW ECO:0000256|RuleBase:RU369109}; Immunity {ECO:0000256|RuleBase:RU369109};
KW Kinase {ECO:0000313|EMBL:EPY88487.1};
KW Lysosome {ECO:0000256|RuleBase:RU369109};
KW Oxidoreductase {ECO:0000256|RuleBase:RU369109};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU369109};
KW Reference proteome {ECO:0000313|Proteomes:UP000030684};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|RuleBase:RU369109};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Signal {ECO:0000256|RuleBase:RU369109};
KW Transferase {ECO:0000313|EMBL:EPY88487.1}.
FT DOMAIN 66..161
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 358..452
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 26..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 182..209
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 657 AA; 75767 MW; 0E5261A4216FB045 CRC64;
MGPRSESRTE PIPDFPALLV EKLLQEHLEE QEVAPPALPP KPPKAKPAST GLANGGNPPS
LQDAEWYWGD ISREEVNEKL RDTPDGTFLV RDASSKIQGE YTLTLRKGGN NKLIKVFHRD
GHYGFSEPLT FCSVVDLITH YRHESLAQYN AKLDTRLLYP VSKYQQDQIV KEDSVEAVGA
QLKVYHQQYQ DKSREYDQLY EEYTRTSQEL QMKRTAIEAF NETIKIFEEQ GQTQEKCSKE
YLERFRREGN EKEMQRILLN SERLKSRIAE IHESRTKLEQ ELRVQASDNR EIDKRMNSLK
PDLMQLRKIR DQYLVWLTQK GARQKKINEW LGIKNETEDQ YSLMEDEDDL PHHEERTWYV
GKINRTQAEE MLSGKRDGTF LIRESSQRGC YACSVVVDGD TKHCVIYRTA TGFGFAEPYN
LYGSLKELVL HYQHASLVQH NDALTVTLAH PAGELCLRAP LGKSDPPPVN VSLYYESLCP
GCRYFLVREL FPTWLLVQEI LNVTLVPYGN AQERNISGKW EFTCQHGEQE CKLNKVEACL
LDQLERNVAF LTIVCLEEMD DMEKNLKPCL QIYAPKVSPD TIMECAMGDR GMQLLHINAQ
LTDALQPPHE YVPWVVVNGK PMKKQGQLLR LVCQLYQGEK PDVCQIMTSS HKEVCFK
//
