STBD1_MOUSE
ID STBD1_MOUSE Reviewed; 338 AA.
AC Q8C7E7; Q147T8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Starch-binding domain-containing protein 1 {ECO:0000303|PubMed:20810658};
DE AltName: Full=Genethonin-1 {ECO:0000303|PubMed:20810658};
DE AltName: Full=Glycophagy cargo receptor stbd1 {ECO:0000305};
GN Name=Stbd1 {ECO:0000303|PubMed:20810658}; Synonyms=D5Ertd593e;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-196; SER-209 AND
RP SER-220, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167 AND SER-223, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DOMAIN, GLYCOGEN-BINDING, AND
RP FUNCTION.
RX PubMed=20810658; DOI=10.1074/jbc.m110.150839;
RA Jiang S., Heller B., Tagliabracci V.S., Zhai L., Irimia J.M.,
RA DePaoli-Roach A.A., Wells C.D., Skurat A.V., Roach P.J.;
RT "Starch binding domain-containing protein 1/genethonin 1 is a novel
RT participant in glycogen metabolism.";
RL J. Biol. Chem. 285:34960-34971(2010).
CC -!- FUNCTION: Acts as a cargo receptor for glycogen. Delivers its cargo to
CC an autophagic pathway called glycophagy, resulting in the transport of
CC glycogen to lysosomes. {ECO:0000250|UniProtKB:O95210,
CC ECO:0000269|PubMed:20810658}.
CC -!- SUBUNIT: Interacts with the ATG8 family proteins GABARAP and GABARAPL1
CC (By similarity). Interacts with several glycogen-associated proteins,
CC such as GYS2 (liver glycogen synthase), GDE (glycogen debranching
CC enzyme), GBE1 (glycogen branching enzyme 1) and EPM2A (Laforin) (By
CC similarity). {ECO:0000250|UniProtKB:O95210}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:Q5FVN1, ECO:0000305|PubMed:20810658}; Single-
CC pass type III membrane protein {ECO:0000250|UniProtKB:O95210}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O95210}; Single-
CC pass type III membrane protein {ECO:0000250|UniProtKB:O95210}. Cell
CC membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O95210}.
CC Note=Also detected near the junctional sarcoplasmic reticulum (By
CC similarity). Concentrates at perinuclear structures (PubMed:20810658).
CC {ECO:0000250|UniProtKB:O95210, ECO:0000269|PubMed:20810658}.
CC -!- TISSUE SPECIFICITY: Expressed at high level in glycogen-accumulating
CC organs such as muscle and liver. Trace signals are also found in brain,
CC kidney, and pancreas. {ECO:0000269|PubMed:20810658}.
CC -!- DOMAIN: The LIR motif (LC3-interacting region) is required for the
CC interaction with the ATG8 family protein GABARAPL1.
CC {ECO:0000250|UniProtKB:O95210}.
CC -!- DOMAIN: The C-terminal CBM20 domain is required for the interaction
CC with glycogen. {ECO:0000269|PubMed:20810658}.
CC -!- PTM: Ubiquitinated, which leads to proteasomal degradation.
CC {ECO:0000250|UniProtKB:O95210}.
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 EMBL; AK050416; BAC34244.1; -; mRNA.
DR EMBL; BC118661; AAI18662.1; -; mRNA.
DR CCDS; CCDS19433.1; -.
DR RefSeq; NP_780305.1; NM_175096.3.
DR AlphaFoldDB; Q8C7E7; -.
DR SMR; Q8C7E7; -.
DR IntAct; Q8C7E7; 1.
DR STRING; 10090.ENSMUSP00000054322; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR iPTMnet; Q8C7E7; -.
DR PhosphoSitePlus; Q8C7E7; -.
DR jPOST; Q8C7E7; -.
DR MaxQB; Q8C7E7; -.
DR PaxDb; Q8C7E7; -.
DR PRIDE; Q8C7E7; -.
DR ProteomicsDB; 258751; -.
DR Antibodypedia; 2375; 126 antibodies from 25 providers.
DR DNASU; 52331; -.
DR Ensembl; ENSMUST00000050952; ENSMUSP00000054322; ENSMUSG00000047963.
DR GeneID; 52331; -.
DR KEGG; mmu:52331; -.
DR UCSC; uc008ydp.1; mouse.
DR CTD; 8987; -.
DR MGI; MGI:1261768; Stbd1.
DR VEuPathDB; HostDB:ENSMUSG00000047963; -.
DR eggNOG; ENOG502SE11; Eukaryota.
DR GeneTree; ENSGT00390000007731; -.
DR HOGENOM; CLU_070592_0_0_1; -.
DR InParanoid; Q8C7E7; -.
DR OMA; NGGVTRW; -.
DR OrthoDB; 1378991at2759; -.
DR PhylomeDB; Q8C7E7; -.
DR TreeFam; TF338505; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 52331; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q8C7E7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8C7E7; protein.
DR Bgee; ENSMUSG00000047963; Expressed in secondary oocyte and 203 other tissues.
DR ExpressionAtlas; Q8C7E7; baseline and differential.
DR Genevisible; Q8C7E7; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISS:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030315; C:T-tubule; ISO:MGI.
DR GO; GO:0038024; F:cargo receptor activity; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:2001069; F:glycogen binding; ISS:GO_Central.
DR GO; GO:0030247; F:polysaccharide binding; ISO:MGI.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005980; P:glycogen catabolic process; ISS:GO_Central.
DR GO; GO:0061723; P:glycophagy; IMP:MGI.
DR GO; GO:0046907; P:intracellular transport; IGI:ParkinsonsUK-UCL.
DR GO; GO:0061753; P:substrate localization to autophagosome; IMP:MGI.
DR CDD; cd05813; CBM20_genethonin_1; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR034838; CBM20_genethonin_1.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00686; CBM_20; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF49452; SSF49452; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 1: Evidence at protein level;
KW Autophagy; Carbohydrate metabolism; Cell membrane; Endoplasmic reticulum;
KW Glycogen metabolism; Membrane; Phosphoprotein; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..338
FT /note="Starch-binding domain-containing protein 1"
FT /id="PRO_0000238961"
FT TOPO_DOM 1..6
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 238..337
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT REGION 30..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 185..191
FT /note="LIR"
FT /evidence="ECO:0000250|UniProtKB:O95210"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5FVN1"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95210"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95210"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95210"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95210"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5FVN1"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 338 AA; 36127 MW; 66C12554D9C9EC59 CRC64;
MGAVWSALLV GGGLAGALIL WLLRGDSGAP GKDGVAEPPQ KGAPPGEAAA PGDGPGGGGS
GGLSPEPSDR ELVSKAEHLR ESNGHLISES KDLGNLPEAQ RLQNVGADWV NAREFVPVGK
IPDTHSRADS EAARNQSPGS HGGEWRLPKG QETAVKVAGS VAAKLPSSSL LVDRAKAVSQ
DQAGHEDWEV VSRHSSWGSV GLGGSLEASR LSLNQRMDDS TNSLVGGRGW EVDGKVASLK
PQQVSIQFQV HYTTNTDVQF IAVTGDHESL GRWNTYIPLH YCKDGLWSHS VFLPADTVVE
WKFVLVENKE VTRWEECSNR FLQTGHEDKV VHGWWGIH
