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   27-MAR-2024, entry version 173.
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.F33C8.1.1; -.
DR   GlyCosmos; Q19981; 17 sites, No reported glycans.
DR   iPTMnet; Q19981; -.
DR   EPD; Q19981; -.
DR   PaxDb; 6239-F33C8-1a; -.
DR   PeptideAtlas; Q19981; -.
DR   GeneID; 181566; -.
DR   KEGG; cel:CELE_F33C8.1; -.
DR   UCSC; F33C8.1b; c. elegans. [Q19981-1]
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; MNGCPSD; -.
DR   PhylomeDB; Q19981; -.
DR   PRO; PR:Q19981; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd00054; EGF_CA; 1.
DR   CDD; cd00055; EGF_Lam; 2.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 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   PANTHER; PTHR46376:SF2; DISTRACTED, ISOFORM B; 1.
DR   PANTHER; PTHR46376; LEUCINE-ZIPPER-LIKE TRANSCRIPTIONAL REGULATOR 1; 1.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF01344; Kelch_1; 3.
DR   Pfam; PF13854; Kelch_5; 1.
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; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF117281; Kelch motif; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 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
//