TAG53_CAEEL
ID TAG53_CAEEL Reviewed; 1329 AA.
AC Q19981; Q8I4J9; Q9BMB0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Putative protein tag-53;
DE Flags: Precursor;
GN Name=tag-53; ORFNames=F33C8.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RA Duke-Cohan J.S., Ashrafi K., Ruvkun G.;
RT "Identification of the correct 3' exon sequence for Caenorhabditis elegans
RT attractin.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103; ASN-555; ASN-832 AND
RP ASN-1147, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q19981-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q19981-2; Sequence=VSP_007250;
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DR EMBL; AF339882; AAK14396.1; -; mRNA.
DR EMBL; Z69790; CAA93653.3; -; Genomic_DNA.
DR EMBL; Z69790; CAD56579.2; -; Genomic_DNA.
DR PIR; T21694; T21694.
DR RefSeq; NP_001024625.2; NM_001029454.4.
DR RefSeq; NP_510443.4; NM_078042.4.
DR AlphaFoldDB; Q19981; -.
DR SMR; Q19981; -.
DR BioGRID; 46463; 5.
DR STRING; 6239.F33C8.1a; -.
DR iPTMnet; Q19981; -.
DR EPD; Q19981; -.
DR PaxDb; Q19981; -.
DR PeptideAtlas; Q19981; -.
DR PRIDE; Q19981; -.
DR GeneID; 181566; -.
DR KEGG; cel:CELE_F33C8.1; -.
DR UCSC; F33C8.1b; c. elegans. [Q19981-1]
DR CTD; 181566; -.
DR WormBase; F33C8.1a; CE41898; WBGene00006432; tag-53. [Q19981-1]
DR WormBase; F33C8.1b; CE41899; WBGene00006432; tag-53. [Q19981-2]
DR eggNOG; KOG1388; Eukaryota.
DR InParanoid; Q19981; -.
DR OMA; EACNIAA; -.
DR OrthoDB; 49565at2759; -.
DR PhylomeDB; Q19981; -.
DR PRO; PR:Q19981; -.
DR Proteomes; UP000001940; Chromosome X.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00055; EGF_Lam; 2.
DR Gene3D; 2.120.10.80; -; 2.
DR Gene3D; 2.60.120.290; -; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF01344; Kelch_1; 2.
DR Pfam; PF00053; Laminin_EGF; 2.
DR Pfam; PF01437; PSI; 1.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00423; PSI; 3.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; EGF-like domain; Glycoprotein;
KW Kelch repeat; Laminin EGF-like domain; Membrane; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..1329
FT /note="Putative protein tag-53"
FT /id="PRO_0000017101"
FT TOPO_DOM ?..1175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1176..1196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1197..1329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 65..92
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 94..203
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 204..232
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 235..270
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 302..353
FT /note="Kelch 1"
FT REPEAT 355..408
FT /note="Kelch 2"
FT REPEAT 416..463
FT /note="Kelch 3"
FT REPEAT 471..518
FT /note="Kelch 4"
FT REPEAT 520..575
FT /note="Kelch 5"
FT REPEAT 577..619
FT /note="Kelch 6"
FT DOMAIN 945..999
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 952..998
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1000..1047
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 832
FT /note="N-linked (GlcNAc...) asparagine; atypical"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 833
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 934
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 973
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1066
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT DISULFID 66..75
FT /evidence="ECO:0000250"
FT DISULFID 70..80
FT /evidence="ECO:0000250"
FT DISULFID 82..91
FT /evidence="ECO:0000250"
FT DISULFID 94..120
FT /evidence="ECO:0000250"
FT DISULFID 144..166
FT /evidence="ECO:0000250"
FT DISULFID 205..215
FT /evidence="ECO:0000250"
FT DISULFID 209..220
FT /evidence="ECO:0000250"
FT DISULFID 222..231
FT /evidence="ECO:0000250"
FT DISULFID 236..252
FT /evidence="ECO:0000250"
FT DISULFID 247..257
FT /evidence="ECO:0000250"
FT DISULFID 259..269
FT /evidence="ECO:0000250"
FT DISULFID 945..953
FT /evidence="ECO:0000250"
FT DISULFID 947..968
FT /evidence="ECO:0000250"
FT DISULFID 971..980
FT /evidence="ECO:0000250"
FT DISULFID 983..997
FT /evidence="ECO:0000250"
FT DISULFID 1000..1009
FT /evidence="ECO:0000250"
FT DISULFID 1002..1016
FT /evidence="ECO:0000250"
FT DISULFID 1018..1028
FT /evidence="ECO:0000250"
FT DISULFID 1031..1045
FT /evidence="ECO:0000250"
FT VAR_SEQ 753..790
FT /note="SPAFFLVHSRRKGKNRDPNQYQAADMSRVPRAAAFNSL -> I (in
FT isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_007250"
SQ SEQUENCE 1329 AA; 146792 MW; F06715D15481925B CRC64;
MLGNITPVSF FKTWVLKKTD VHVMISAREV FPCFIFRVFL LFQVFSRVHT LTNHANFEFE
KSLSSCDKPC YNGVCLNKAC VCSKGWYGSQ CDHCFGRIRI SDNASYISDG PLDYSPSAKC
TWLIEPENSA TPLKIRINSF FTECGWDYLY IYDGDSVYGK QLAALCGEQP SQEFTAASGK
ALVHFFSDLA INLNGFNVSY ESNRCAYNCS NHGSCLNGKC DCEDGYKGLN CEYQVCQLSG
KSTESPCHEG QCVDGRCECL SARVHGETCQ MPVSSSVWDL IHPTNNAPTG KASHASIAID
DVVWSIGGEF FDGSSDPNNI DVYNVTSRIW SKVEVSGDMP KPRFDHTVVK YKNKLYMFGG
VTKTQVRHQT TQAATNELWI FDMGSKKWAQ QIHKNETIIA APFAVAGHSA HVIRSEMFVI
FGYNPLFGFM HHVQIYNFET EEWTVANTSD HVYGRFKHSA VEYTTPTGAT AILVYGGSMW
NNTITDSLMQ FDTSTKKWSN LPQSGVQLYL HAAAYLNGLM VVVGGRGSNV TAGSKSECFS
NMVQSYDVAC KQWSNMSTAP VDLKRFGHSV HVIGQKLYAL GGFNGKMKSD VWTLSPAKCS
SATRPDECRL ITDGTKCVFV DSSCVPFDPT VSYKSSFASM IKSSTPKSFD ECTNTPLRLA
LKTCEEQTDC VSCASKSGCG WCSSGEQCLP NEQECVDGPG MLTSWEKCPQ RNSVATMRPC
NMENNCGSCR ISPHCTWYPI DKASPCVSKE DLSPAFFLVH SRRKGKNRDP NQYQAADMSR
VPRAAAFNSL AVVYEYETKS VLADRNKFLS PSHFPSFFRN ATECPMPCAQ RNNCSDCTDL
EQCMWCPSTN RCINLEAYTL SFAYGQCHSW VTSGSGSVIN RVCQAESVVC EEHKTCGECQ
RDPGCGWLAD DSKTGLGLCI RGTSTGPLEP KPENSTWYFI DCPACQCNGH STCFTSVGSF
PPVTIEKCQS CQNHTTGAHC ERCAPGFYGD ARNGGVCSPC DCHHQADMCD PVSGQCFCKT
KGVTGDRCDK CEAKYVGNPR NGTPCFYELA VDFIFTFKLR SDDKDNHTSE IYLYSVPYKK
DTDVTFQISC ESPKGNALVA LNMTSSYVNG LADKSQAMMV DTICDSKGFR RVYVASDKGY
PFGPDSNTTF FVRVYNFNTP VQIVVSFAQS PPINWVLFFV IFAACFIVLL VVAGLLWMIK
VRIEAYRRNQ RRIDEIEHMA SRPFASTKME LSMLSQFSSA GGPTPLSIEP CSNYRAGVFT
LAVRLPTGGK AVTPSGTSGL AVASSLCLLT PQQVGVLQAQ DNGESNSGRK SNFRNLLRLT
IRQRPNNND
