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Database: UniProt
Entry: Q21281
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ID   MUP4_CAEEL              Reviewed;        2104 AA.
AC   Q21281; Q964N4;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 4.
DT   16-JAN-2019, entry version 157.
DE   RecName: Full=Transmembrane matrix receptor MUP-4 {ECO:0000312|EMBL:AAK69172.1};
DE   AltName: Full=Muscle-positioning protein 4;
DE   Flags: Precursor;
GN   Name=mup-4 {ECO:0000312|EMBL:CCD63613.1,
GN   ECO:0000312|WormBase:K07D8.1}; ORFNames=K07D8.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAK69172.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=11470827; DOI=10.1083/jcb.200007075;
RA   Hong L., Elbl T., Ward J., Franzini-Armstrong C., Rybicka K.K.,
RA   Gatewood B.K., Baillie D.L., Bucher E.A.;
RT   "MUP-4 is a novel transmembrane protein with functions in epithelial
RT   cell adhesion in Caenorhabditis elegans.";
RL   J. Cell Biol. 154:403-414(2001).
RN   [2] {ECO:0000312|EMBL:CCD63613.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD63613.1};
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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [3] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9136009;
RA   Gatewood B.K., Bucher E.A.;
RT   "The mup-4 locus in Caenorhabditis elegans is essential for hypodermal
RT   integrity, organismal morphogenesis and embryonic body wall muscle
RT   position.";
RL   Genetics 146:165-183(1997).
CC   -!- FUNCTION: Required for junctional attachments between hypodermis
CC       and muscle, and between the apical epithelial surface and the
CC       cuticular matrix. Essential for enclosure of the embryo by the
CC       hypodermis, hypodermal integrity, embryo elongation, and
CC       maintenance of hypodermal morphology in fully elongated embryos.
CC       {ECO:0000269|PubMed:11470827, ECO:0000269|PubMed:9136009}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, hemidesmosome
CC       {ECO:0000269|PubMed:11470827}. Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:11470827}. Cell membrane {ECO:0000255};
CC       Single-pass membrane protein {ECO:0000255}. Note=Detected in
CC       intermediate filaments and hemidesmosomes. {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Abundant at hypodermal cell-matrix junctions
CC       overlying muscle of threefold embryos. Expression continues in
CC       body wall muscle in larvae and adults and is also detected in
CC       other regions where cells show mechanical attachment to the
CC       hypodermis including the inner surface of the pharynx, overlying
CC       anal and intestinal muscles, overlying vulval and uterine sex
CC       muscles, male tail muscle attachment zones and the six
CC       mechanosensory neurons (at protein level).
CC       {ECO:0000269|PubMed:11470827}.
CC   -!- DEVELOPMENTAL STAGE: Expression detected in embryo, larva and
CC       adult. {ECO:0000269|PubMed:11470827}.
CC   -!- DISRUPTION PHENOTYPE: Arrested embryonic development either at
CC       bean or twofold stages with failure of hypodermis to enclose the
CC       embryo or at threefold stage with defects in hypodermal cell
CC       organization and muscle cell positioning. When disrupted in
CC       larvae, causes paralysis and displacement of muscles.
CC       {ECO:0000269|PubMed:11470827, ECO:0000269|PubMed:9136009}.
DR   EMBL; AF289202; AAK69172.1; -; mRNA.
DR   EMBL; FO080425; CCD63613.1; -; Genomic_DNA.
DR   RefSeq; NP_498645.1; NM_066244.6.
DR   UniGene; Cel.17092; -.
DR   ProteinModelPortal; Q21281; -.
DR   SMR; Q21281; -.
DR   BioGrid; 41268; 10.
DR   DIP; DIP-26346N; -.
DR   IntAct; Q21281; 2.
DR   STRING; 6239.K07D8.1; -.
DR   EPD; Q21281; -.
DR   PaxDb; Q21281; -.
DR   PeptideAtlas; Q21281; -.
DR   PRIDE; Q21281; -.
DR   EnsemblMetazoa; K07D8.1; K07D8.1; WBGene00003497.
DR   GeneID; 176060; -.
DR   KEGG; cel:CELE_K07D8.1; -.
DR   UCSC; K07D8.1.1; c. elegans.
DR   CTD; 176060; -.
DR   WormBase; K07D8.1; CE29511; WBGene00003497; mup-4.
DR   eggNOG; ENOG410IR5K; Eukaryota.
DR   eggNOG; ENOG410ZJKT; LUCA.
DR   GeneTree; ENSGT00940000167387; -.
DR   HOGENOM; HOG000018807; -.
DR   InParanoid; Q21281; -.
DR   OMA; CGLCNGH; -.
DR   OrthoDB; 1174178at2759; -.
DR   PhylomeDB; Q21281; -.
DR   Reactome; R-CEL-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-CEL-8957275; Post-translational protein phosphorylation.
DR   PRO; PR:Q21281; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00003497; Expressed in 4 organ(s), highest expression level in multi-cellular organism.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030056; C:hemidesmosome; IDA:WormBase.
DR   GO; GO:0098733; C:hemidesmosome associated protein complex; IDA:WormBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR006150; Cys_repeat_1.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024731; EGF_dom.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR000082; SEA_dom.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF07645; EGF_CA; 7.
DR   Pfam; PF12661; hEGF; 3.
DR   Pfam; PF00092; VWA; 1.
DR   SMART; SM00181; EGF; 27.
DR   SMART; SM00179; EGF_CA; 19.
DR   SMART; SM00200; SEA; 2.
DR   SMART; SM00327; VWA; 1.
DR   SMART; SM00289; WR1; 3.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 13.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 21.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS50024; SEA; 2.
DR   PROSITE; PS50234; VWFA; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Cell junction; Cell membrane;
KW   Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     15       {ECO:0000255}.
FT   CHAIN        16   2104       Transmembrane matrix receptor MUP-4.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000423668.
FT   TOPO_DOM     16   1860       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1861   1881       Helical. {ECO:0000255}.
FT   TOPO_DOM   1882   2104       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       71    110       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      122    163       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      175    213       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      220    265       WR1. {ECO:0000255}.
FT   DOMAIN      278    315       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      327    360       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      377    416       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      437    612       VWFA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN      728    772       EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      819    857       EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      869    907       EGF-like 9; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      919    958       EGF-like 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      968   1007       EGF-like 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1016   1058       EGF-like 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1071   1110       EGF-like 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1121   1160       EGF-like 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1169   1208       EGF-like 15. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1215   1254       EGF-like 16. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1322   1444       SEA 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00188}.
FT   DOMAIN     1495   1620       SEA 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00188}.
FT   DOMAIN     1622   1658       EGF-like 17. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1669   1705       EGF-like 18. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1717   1754       EGF-like 19. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1772   1810       EGF-like 20; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1817   1853       EGF-like 21. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   CARBOHYD    494    494       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    556    556       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    879    879       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1037   1037       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1132   1132       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1271   1271       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1403   1403       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1576   1576       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1730   1730       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1782   1782       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1838   1838       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     75     89       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     83     98       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    126    142       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    136    151       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    179    192       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    186    201       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    282    294       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    288    303       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    331    344       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    338    353       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    355    359       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    381    395       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    389    404       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    732    746       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    740    756       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    758    771       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    823    836       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    830    845       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    873    886       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    880    895       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    923    937       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    931    946       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    972    985       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    979    995       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1020   1034       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1028   1046       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1075   1089       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1083   1098       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1125   1139       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1133   1148       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1173   1187       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1181   1196       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1219   1233       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1227   1242       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1626   1637       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1631   1646       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1673   1687       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1681   1696       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1721   1733       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1727   1742       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1776   1789       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1783   1798       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1821   1830       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1824   1841       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1843   1852       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   CONFLICT    919    919       L -> P (in Ref. 1; AAK69172).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2104 AA;  230054 MW;  C98CD462CC434F8B CRC64;
     MRWVPLVLLP LIASAATTYQ HRQTYSSLQC RVNDPLSCNQ AKSEVCVFVN GQYRCECPVG
     VSRLADGRCL VVNECARPSL NACHKDAQCV DLAEGYTCRC NSGFADTSPD KVNKPGRQCQ
     KTTNECGAKQ TYGVDCDENA ACVDTPEGFQ CVCQPGYADV STSISKLPGR KCVESVNECT
     NGEADCSNNA DCFDRADGYE CKCRPGFVDA SPNVDKYPGR VCNKPKAPEY YGQQSRQPQC
     SEGSGCGPNE ECRFNTAGEK VCQCRRGSVQ QSNGVCKVFS QCEQANECDR NAFCSNTYDG
     PKCQCKDGFL DVSPDPVRLP GRKCQQVRNE CADGSHDCSH QAACQDTPTG YICSCNSNCI
     DVSSRYNLPP GRKCSVAANQ CSDKSLNSCD ENADCVQLPD GYTCKCFAGY VDVSSNANLP
     PGRVCTLSTA CPAQPTDLVF LIDGSGSIGS YVFQTEVLRF LAEFTELFDI APQKTRVSVV
     QYSDQIRHEF GLDNYSDRKS LQNAIRNIEY LTGLTRTGAA IEHVANEAFS ERRGARPVGQ
     VSRVAIVITD GRSQDNVTRP SDNARRQDIQ LFAVGVTNHV LDAELEEISG SKDRTFHVSG
     FEDLNTRLRS AIQRVACPHQ NNEDTYNKGP CDPSNHNGCD RSLNQVCQQK NGKFVCACPA
     GFDIHPVTKV CGGDICNPEI ATSCPDPEIC EKTPFGNWRC TCPADLGWRD RLTGVCKIGE
     KPVQTSESND ECSPNDVHSC PANSKCEKGA GGEFICKCDA GFQRNGRTNK CEAPGTCDPR
     MPDSCDARKK EKCLPDGRGA FACMCDRHHK RHPVTDICLI DECAAGVADC DPNAKCTDTD
     ESYICTCNEG FLDKSPEQNK KPGRVCSKQR NECLDGTHNC SMNADCIDLP DGFLCRCKED
     FVDISPNPNA FGGIDCRALV NECLITGGHN CHEHAICIDT RDSYKCQCKE GYVDHDELRN
     PGRTCKKLNQ ICESGKHECD KNARCVEKGA NDYECVCNAG FIDKSPLTHR PGRKCVEPIC
     SDDSKHDCHS AAICEENDSV PEKYTCKCRD GYLDVGAVMG GGKSGRECKE LVNECLSASL
     NSCDAAATCI DLDDGYTCKC PLGSKDESPV PKLPGRSCKG LVNECNIPHL NNCSHFATCI
     DLEEGYECKC KPEYHDQKPE QPGTECKFII NECLAENLND CSPNAMCIDK IDGYDCKCKA
     PFQDEMPSNP GRICRFDECA DPKDNDCDKH ALCIDTDDSY TCQCKEGFFD EISDPKKPGR
     VCIGLVIEPQ NQSEDPTTPD PNTIKCGNGL CHLDLGEVCV GGATCSCRPG ESRDNEKEKC
     VPTTSIPLVV RVMEYDGEPI QYRTDYSKPD TQAHIEIVDA VKKSVGKIIG KTDVAPRFVT
     TDVNYITNPK VQNSEWDKGL LGNVSVHLAG KEEVDKCRFY EQFAEIVREM GGRVDRIKLS
     DDADLDPCKK EEEKKGIPCG NTFCSIELGE ECIAGKICGC PKGQKRKDAN SPCRAVESWN
     LPLYVIRDGH EKITYSPSLS NPLNDDHKDL VSRFESGVAQ SYDKTPLKGA FVTAEVNEIE
     NPESRKKSWD TGILYNFTSH FVKGSVAEPA SVFTDLIDYI QKRNDFEVGK SKLFISPEQL
     NPFSNCYHSD CHPDAICKEV GKGYTCTCPD GFRDLNPSRP GRNCLSYRGV NECEKPELNE
     CSPHARCIDL DYLYKCECIR PYVNSAVGDA LPGSVCSIDY CQDVNYCPLN STCVNVDEQA
     RCDCKPGFVD LRKSGHLSEA GLGESICRRQ SDIDECALGL HNCSAAAICI DKKIGYECQC
     QEGYEDGNPS QPGRICAASL CGLCNGHGDC IHDALSSNVT CACLDGYTGQ FCETAPSNLP
     LILMTLLALL FLLLTLLCCL YMCARCRCFG ARGRSEGSAS GQEILGSDYY TIPRAKLARP
     LYGDEMGDDH AGALAAYLDD GASISSDGSI EEIERRVTTD VTTREVRTTT VRDDDGNIIS
     QSQTISHGNP HETDTEQYGM ISSDHYKTSA SEAMDAAMST SASGAAYNQS SGAMMSSASG
     HKSAYNQGYA SDSEDSDAGH AVYDRTTRTN QSHDFEPGAD PRTGTERSKR EFVTTTKAEE
     VNYF
//
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