ID   B1WC34_RAT              Unreviewed;       525 AA.
AC   B1WC34;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=Glucosidase 2 subunit beta {ECO:0000256|ARBA:ARBA00022387};
GN   Name=Prkcsh {ECO:0000313|Ensembl:ENSRNOP00000018009.5,
GN   ECO:0000313|RGD:1309628};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000018009.5, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000018009.5, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000018009.5,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000018009.5}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000018009.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; NP_001100276.1; NM_001106806.2.
DR   RefSeq; XP_006242695.1; XM_006242633.3.
DR   AlphaFoldDB; B1WC34; -.
DR   SMR; B1WC34; -.
DR   STRING; 10116.ENSRNOP00000018009; -.
DR   PhosphoSitePlus; B1WC34; -.
DR   PaxDb; 10116-ENSRNOP00000018009; -.
DR   Ensembl; ENSRNOT00000018009.7; ENSRNOP00000018009.5; ENSRNOG00000013360.7.
DR   GeneID; 300445; -.
DR   KEGG; rno:300445; -.
DR   UCSC; RGD:1309628; rat.
DR   AGR; RGD:1309628; -.
DR   CTD; 5589; -.
DR   RGD; 1309628; Prkcsh.
DR   eggNOG; KOG2397; Eukaryota.
DR   GeneTree; ENSGT00510000047770; -.
DR   HOGENOM; CLU_016834_1_0_1; -.
DR   OMA; YENGQHC; -.
DR   OrthoDB; 103990at2759; -.
DR   TreeFam; TF329550; -.
DR   Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000013360; Expressed in ovary and 20 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0017177; C:glucosidase II complex; ISO:RGD.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR   GO; GO:0051219; F:phosphoprotein binding; ISO:RGD.
DR   GO; GO:0005080; F:protein kinase C binding; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:0003723; F:RNA binding; ISO:RGD.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR   GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR   GO; GO:0001889; P:liver development; ISO:RGD.
DR   GO; GO:0006491; P:N-glycan processing; ISO:RGD.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; ISO:RGD.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; ISO:RGD.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR   Gene3D; 2.70.130.10; Mannose-6-phosphate receptor binding domain; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR039794; Gtb1-like.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR   InterPro; IPR044865; MRH_dom.
DR   InterPro; IPR036607; PRKCSH.
DR   InterPro; IPR028146; PRKCSH_N.
DR   PANTHER; PTHR12630:SF1; GLUCOSIDASE 2 SUBUNIT BETA; 1.
DR   PANTHER; PTHR12630; N-LINKED OLIGOSACCHARIDE PROCESSING; 1.
DR   Pfam; PF13202; EF-hand_5; 1.
DR   Pfam; PF12999; PRKCSH-like; 1.
DR   Pfam; PF13015; PRKCSH_1; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF50911; Mannose 6-phosphate receptor domain; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS51914; MRH; 1.
PE   1: Evidence at protein level;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   REGION          176..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          282..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          364..394
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        305..329
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..349
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   525 AA;  59218 MW;  C9C1089E36012BE8 CRC64;
     MLLLLLLLPL CWAVEVKRPR GVSLSNHHFY DESKPFTCLD GTATIPFDQV NDDYCDCKDG
     SDEPGTAACP NGSFHCTNTG YKPLYILSSR VNDGVCDCCD GTDEYNSGTV CENTCREKGR
     KEKESLQQLA EVTREGFRLK KILIEEWKTA REEKQSKLLE LQAGKKSLED QVETLRTAKE
     EAERPEKEAK DQHRKLWEEQ QAAAKARREQ ELAASAFQEL DDNMDGLVSL AELQTHPELD
     TDGDGGLSEE EAQALLSGDT QTDTTSFYDR VWAAIRDKYR SEVPPTDIPV PEVTEPKEEK
     LPVLPPMEEE EEEEEPEEEE EEEEEEVPGE QPKEVPPPQQ PLRPPSPAED EKMPPYDEET
     QAIIDAAQEA RNKFEEVERS LKEMEESIRS LEQEISFDFG PSGEFAYLYS QCYELTTNEY
     VYRLCPFKLV SQKPKHGGSP TSLGTWGSWA GPDDDKFSAM KYEQGTGCWQ GPNRSTTVRL
     LCGKETVVTS TTEPSRCEYL MELMTPAACP EPPPEVPTDG DHDEL
//