YMS5_CAEEL
ID YMS5_CAEEL Reviewed; 1385 AA.
AC P34501;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Uncharacterized protein K03H1.5;
DE Flags: Precursor;
GN ORFNames=K03H1.5;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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-313; ASN-386; ASN-562 AND
RP ASN-1225, 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).
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DR EMBL; Z29560; CAA82664.1; -; Genomic_DNA.
DR PIR; H88569; H88569.
DR PIR; S41028; S41028.
DR RefSeq; NP_499205.1; NM_066804.4.
DR AlphaFoldDB; P34501; -.
DR SMR; P34501; -.
DR STRING; 6239.K03H1.5; -.
DR iPTMnet; P34501; -.
DR EPD; P34501; -.
DR PaxDb; P34501; -.
DR PeptideAtlas; P34501; -.
DR EnsemblMetazoa; K03H1.5.1; K03H1.5.1; WBGene00010540.
DR GeneID; 176404; -.
DR KEGG; cel:CELE_K03H1.5; -.
DR UCSC; K03H1.5; c. elegans.
DR CTD; 176404; -.
DR WormBase; K03H1.5; CE03459; WBGene00010540; -.
DR eggNOG; KOG4291; Eukaryota.
DR GeneTree; ENSGT00730000110943; -.
DR HOGENOM; CLU_003648_1_0_1; -.
DR InParanoid; P34501; -.
DR OMA; YFRMERD; -.
DR OrthoDB; 668024at2759; -.
DR PhylomeDB; P34501; -.
DR Reactome; R-CEL-913709; O-linked glycosylation of mucins.
DR PRO; PR:P34501; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00010540; Expressed in material anatomical entity and 4 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR CDD; cd00033; CCP; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR005533; AMOP_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR003886; NIDO_dom.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR001846; VWF_type-D.
DR Pfam; PF03782; AMOP; 1.
DR Pfam; PF06119; NIDO; 1.
DR Pfam; PF00084; Sushi; 1.
DR Pfam; PF00094; VWD; 1.
DR SMART; SM00723; AMOP; 1.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00429; IPT; 1.
DR SMART; SM00539; NIDO; 1.
DR SMART; SM00216; VWD; 1.
DR SUPFAM; SSF57535; SSF57535; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50856; AMOP; 1.
DR PROSITE; PS51220; NIDO; 1.
DR PROSITE; PS50923; SUSHI; 1.
DR PROSITE; PS51233; VWFD; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Reference proteome; Signal; Sushi.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1385
FT /note="Uncharacterized protein K03H1.5"
FT /id="PRO_0000014290"
FT DOMAIN 285..450
FT /note="NIDO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT DOMAIN 681..840
FT /note="AMOP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00347"
FT DOMAIN 852..1088
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1179..1238
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 234..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1353
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 909
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 921
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 975
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1009
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT DISULFID 1181..1223
FT /evidence="ECO:0000250"
FT DISULFID 1209..1236
FT /evidence="ECO:0000250"
SQ SEQUENCE 1385 AA; 159182 MW; BDCD8F59CEA38C03 CRC64;
MWTARHAVAL LVVLTYAYSS ILPPGTTFVQ SIRDIFRFQE QLKKENVEDT ICSETPPESS
IPNRDELLEL IRKSKIEDHK FDEHVRKKRQ LSRISYQEYL DNLGKADYDV RIEEGWTEIL
YPFGTWAMDK QLMGQAGRET QTNLGFDCPF FGFRFNYTMV YPMGMLSFGL PPFSAPPWTF
PNPAWPKQRD HSFVAAFYAD AMFQWIGNTK ISNVFFRSVH RPRLDDDEVY ERNSQTNYGA
PNYQQAGAQS AANQQFSNPS QYSQNLNAYS QNQQYNTQLL QQQQQIYGKR KKRQMPGRVS
QPGMVVDPWL LDNITRHIQD GYTGANGFRA EHAFIATWYR MAHGGAARAL DVSQFEHVKD
WQNTFQVVLA SDEIRTFAIF NYARLNWTSS NEAGGLDGFG GKQAAMAGFN GGNGTGWYGL
PYSGEGRLWK LGYFSNVLTP GRWIHRVDEV IIPAGCTNAS NGGMMTAPPW GPMHGGMAIN
VSGPCLRPAD SVKVNFENWQ TSCTRLSRVR ARCIMPMFHK IGLVPIRMSR DGGQSFPFFG
KFYVVNSERA PASVSLKDSV DNKTNRWYEP YAQELALGWQ AMNLTWNTGA RVDISLFGYW
EDADRSHFER IDYLARGISN TGSYSFRPQQ LTKQFLLRDA WQKFHFGFVQ VALADAEDGV
MWSKPTPFPW YHLHEWERYY GRNWPIDMCI EWFEYDGKRN NFQIDLTTDF PCPCKLPQAM
LDLGRFMPIM DCDKDGDTSC PFNKGAQHCI QSVQPTFSGS SQQCCYDYDG YLMFTDDWEP
DGDYTTFFQP GTPARAHRYG AAPYRLPPFI PTLSNYQLDL NPYRTCCKYA DHCEFYYWRR
MTNGCQDYRA PAAGYIYGEP HVITYDGIRY TMPGKGYYVL TMSDSPYHKL MVQVRLEQPD
DTLWHAHVNA TVITGVAVQE NDSSIVQVYA RKPMRRWRYR TDVYVDGTRR FFDKPHWKHQ
QFKHLDIRNP LQNMNQSEIV IMLKSGVGIR IFEGFGMLDV MVTLPPSYNT TCRPGESLSS
SLNAPRGQRR CYTTLGLLGT YNNDPADDLT TPSGTVTRVQ NPTTTASTTQ MIYEQFASFW
KIDGTNDKIG GVLFQDKFKP IYNPLLFAES DYRPVYWPQT IDMNASRVFT MEQVVSTCQN
NPECEYDFIM TGRKEVGLTT LRRQKEFFAL QKTGSKQLIS CGPLLKKEGV VKTPPAANYL
DGDKVVFSCK PKYYIHGDIE RVCRNGTWSP GWWAWCRDRN LEYALKWMTA LLSIFGISLI
FVIFFCILWN IRKKKQAAHA ERLQLKEQSD RLNKLENERI FGTSPEKTPL IETDFRSNFN
MNQPSRPIPS QPPSSQYSPP VFAAPPPPSQ PTRLPTYTNA ISQQQRQFEP PRPPRGNMRF
ETSAI
