STBD1_HUMAN
ID STBD1_HUMAN Reviewed; 358 AA.
AC O95210; B3KVZ9;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 164.
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}; ORFNames=GENX-3414;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Muscle;
RX PubMed=9794794; DOI=10.1042/bj3350549;
RA Bouju S., Lignon M.-F., Pietu G., Le Cunff M., Leger J.-J., Auffray C.,
RA Dechesne C.A.;
RT "Molecular cloning and functional expression of a novel human gene encoding
RT two 41-43 kDa skeletal muscle internal membrane proteins.";
RL Biochem. J. 335:549-556(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP INTERACTION WITH GABARAP AND GABARAPL1, DOMAIN, SUBCELLULAR LOCATION,
RP FUNCTION, GLYCOGEN-BINDING, AND MUTAGENESIS OF TRP-293.
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).
RN [7]
RP INTERACTION WITH GABARAPL1, DOMAIN, MUTAGENESIS OF TRP-203 AND VAL-206,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=21893048; DOI=10.1016/j.bbrc.2011.08.106;
RA Jiang S., Wells C.D., Roach P.J.;
RT "Starch-binding domain-containing protein 1 (Stbd1) and glycogen
RT metabolism: Identification of the Atg8 family interacting motif (AIM) in
RT Stbd1 required for interaction with GABARAPL1.";
RL Biochem. Biophys. Res. Commun. 413:420-425(2011).
RN [8]
RP DOMAIN, GLYCOGEN-BINDING, MUTAGENESIS OF TRP-293, UBIQUITINATION,
RP SUBCELLULAR LOCATION, INTERACTION WITH GYS2; AGL; GBE1 AND EPM2A, AND
RP FUNCTION.
RX PubMed=24837458; DOI=10.1042/bsr20140053;
RA Zhu Y., Zhang M., Kelly A.R., Cheng A.;
RT "The carbohydrate-binding domain of overexpressed STBD1 is important for
RT its stability and protein-protein interactions.";
RL Biosci. Rep. 34:0-0(2014).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-188; SER-194;
RP SER-210; SER-211 AND SER-220, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP 3D-STRUCTURE MODELING OF 260-358, AND PUTATIVE FUNCTION OF STARCH-BINDING
RP DOMAIN.
RX PubMed=12424126; DOI=10.1093/bioinformatics/18.11.1534;
RA Janecek S.;
RT "A motif of a microbial starch-binding domain found in human genethonin.";
RL Bioinformatics 18:1534-1537(2002).
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:0000269|PubMed:20810658,
CC ECO:0000269|PubMed:21893048, ECO:0000269|PubMed:24837458}.
CC -!- SUBUNIT: Interacts with the ATG8 family proteins GABARAP and GABARAPL1
CC (PubMed:20810658, PubMed:21893048). Interacts with several glycogen-
CC associated proteins, such as GYS2 (liver glycogen synthase), GDE
CC (glycogen debranching enzyme), GBE1 (glycogen branching enzyme 1) and
CC EPM2A (Laforin) (PubMed:24837458). {ECO:0000269|PubMed:20810658,
CC ECO:0000269|PubMed:21893048, ECO:0000269|PubMed:24837458}.
CC -!- INTERACTION:
CC O95210; O95166: GABARAP; NbExp=6; IntAct=EBI-2947137, EBI-712001;
CC O95210; Q9H0R8: GABARAPL1; NbExp=8; IntAct=EBI-2947137, EBI-746969;
CC O95210; P60520: GABARAPL2; NbExp=5; IntAct=EBI-2947137, EBI-720116;
CC O95210; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-2947137, EBI-749265;
CC O95210; Q9GZQ8: MAP1LC3B; NbExp=2; IntAct=EBI-2947137, EBI-373144;
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:20810658, ECO:0000305|PubMed:21893048}; Single-pass
CC type III membrane protein {ECO:0000305|PubMed:9794794}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:24837458}; Single-pass type III
CC membrane protein {ECO:0000305|PubMed:9794794}. Cell membrane,
CC sarcolemma, T-tubule {ECO:0000269|PubMed:9794794}. Note=Also detected
CC near the junctional sarcoplasmic reticulum (PubMed:9794794).
CC Concentrates at perinuclear structures (PubMed:21893048).
CC {ECO:0000269|PubMed:21893048, ECO:0000269|PubMed:9794794}.
CC -!- TISSUE SPECIFICITY: Expressed at high level in skeletal and cardiac
CC muscles. Moderately expressed in liver and placenta. No expression is
CC found in pancreas, kidney or lung. Present in skeletal muscle, heart
CC and placenta (at protein level). {ECO:0000269|PubMed:9794794}.
CC -!- DOMAIN: The LIR motif (LC3-interacting region) is required for the
CC interaction with the ATG8 family protein GABARAPL1.
CC {ECO:0000269|PubMed:21893048}.
CC -!- DOMAIN: The C-terminal CBM20 domain is required for the interaction
CC with glycogen and glycogen-associated proteins.
CC {ECO:0000269|PubMed:20810658, ECO:0000269|PubMed:24837458}.
CC -!- PTM: Ubiquitinated, which leads to proteasomal degradation.
CC {ECO:0000269|PubMed:24837458}.
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DR EMBL; AF062534; AAC78827.1; -; mRNA.
DR EMBL; AK123795; BAG53961.1; -; mRNA.
DR EMBL; CH471057; EAX05783.1; -; Genomic_DNA.
DR EMBL; BC022301; AAH22301.1; -; mRNA.
DR CCDS; CCDS3578.1; -.
DR RefSeq; NP_003934.1; NM_003943.4.
DR AlphaFoldDB; O95210; -.
DR SMR; O95210; -.
DR BioGRID; 114469; 128.
DR IntAct; O95210; 28.
DR MINT; O95210; -.
DR STRING; 9606.ENSP00000237642; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR TCDB; 9.B.207.1.1; the starch-binding domain-containing protein, stbd1 (stbd1) family.
DR iPTMnet; O95210; -.
DR PhosphoSitePlus; O95210; -.
DR BioMuta; STBD1; -.
DR EPD; O95210; -.
DR jPOST; O95210; -.
DR MassIVE; O95210; -.
DR MaxQB; O95210; -.
DR PaxDb; O95210; -.
DR PeptideAtlas; O95210; -.
DR PRIDE; O95210; -.
DR ProteomicsDB; 50720; -.
DR Antibodypedia; 2375; 126 antibodies from 25 providers.
DR DNASU; 8987; -.
DR Ensembl; ENST00000237642.7; ENSP00000237642.6; ENSG00000118804.9.
DR GeneID; 8987; -.
DR KEGG; hsa:8987; -.
DR MANE-Select; ENST00000237642.7; ENSP00000237642.6; NM_003943.5; NP_003934.1.
DR UCSC; uc003hka.4; human.
DR CTD; 8987; -.
DR DisGeNET; 8987; -.
DR GeneCards; STBD1; -.
DR HGNC; HGNC:24854; STBD1.
DR HPA; ENSG00000118804; Tissue enhanced (liver, skeletal muscle, tongue).
DR MIM; 607406; gene.
DR neXtProt; NX_O95210; -.
DR OpenTargets; ENSG00000118804; -.
DR PharmGKB; PA162405002; -.
DR VEuPathDB; HostDB:ENSG00000118804; -.
DR eggNOG; ENOG502SE11; Eukaryota.
DR GeneTree; ENSGT00390000007731; -.
DR HOGENOM; CLU_070592_0_0_1; -.
DR InParanoid; O95210; -.
DR OMA; NGGVTRW; -.
DR OrthoDB; 1378991at2759; -.
DR PhylomeDB; O95210; -.
DR TreeFam; TF338505; -.
DR PathwayCommons; O95210; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR SignaLink; O95210; -.
DR BioGRID-ORCS; 8987; 8 hits in 962 CRISPR screens.
DR GenomeRNAi; 8987; -.
DR Pharos; O95210; Tbio.
DR PRO; PR:O95210; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O95210; protein.
DR Bgee; ENSG00000118804; Expressed in gastrocnemius and 98 other tissues.
DR Genevisible; O95210; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0016020; C:membrane; IDA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030315; C:T-tubule; IDA:ParkinsonsUK-UCL.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0038024; F:cargo receptor activity; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:2001069; F:glycogen binding; IDA:GO_Central.
DR GO; GO:0030247; F:polysaccharide binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005980; P:glycogen catabolic process; IMP:GO_Central.
DR GO; GO:0061723; P:glycophagy; IMP:GO_Central.
DR GO; GO:0046907; P:intracellular transport; IGI:ParkinsonsUK-UCL.
DR GO; GO:0061753; P:substrate localization to autophagosome; IEA:Ensembl.
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..358
FT /note="Starch-binding domain-containing protein 1"
FT /id="PRO_0000087476"
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..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 258..357
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT REGION 30..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 200..206
FT /note="LIR"
FT /evidence="ECO:0000305|PubMed:21893048"
FT COMPBIAS 122..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5FVN1"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C7E7"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MUTAGEN 203
FT /note="W->A: Abolishes interaction with GABARAPL1."
FT /evidence="ECO:0000269|PubMed:21893048"
FT MUTAGEN 206
FT /note="V->A: Abolishes interaction with GABARAPL1."
FT /evidence="ECO:0000269|PubMed:21893048"
FT MUTAGEN 293
FT /note="W->G,L: Abolishes GYS2- and glycogen-binding, and
FT leads to rapid degradation."
FT /evidence="ECO:0000269|PubMed:20810658,
FT ECO:0000269|PubMed:24837458"
SQ SEQUENCE 358 AA; 39007 MW; 9C98018B82B1578C CRC64;
MGAVWSALLV GGGLAGALFV WLLRGGPGDT GKDGDAEQEK DAPLGGAAIP GGHQSGSSGL
SPGPSGQELV TKPEHLQESN GHLISKTKDL GKLQAASWRL QNPSREVCDN SREHVPSGQF
PDTEAPATSE TSNSRSYSEV SRNESLESPM GEWGFQKGQE ISAKAATCFA EKLPSSNLLK
NRAKEEMSLS DLNSQDRVDH EEWEMVPRHS SWGDVGVGGS LKAPVLNLNQ GMDNGRSTLV
EARGQQVHGK MERVAVMPAG SQQVSVRFQV HYVTSTDVQF IAVTGDHECL GRWNTYIPLH
YNKDGFWSHS IFLPADTVVE WKFVLVENGG VTRWEECSNR FLETGHEDKV VHAWWGIH
