GenomeNet

Database: UniProt
Entry: Q55AP8
LinkDB: Q55AP8
Original site: Q55AP8 
ID   COMC_DICDI              Reviewed;        1501 AA.
AC   Q55AP8;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   23-MAY-2018, entry version 77.
DE   RecName: Full=EGF-like domain-containing protein comC;
DE   AltName: Full=Communication mutant protein C;
DE   Flags: Precursor;
GN   Name=comC; ORFNames=DDB_G0271692;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A.,
RA   Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G.,
RA   Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A.,
RA   Platzer M., Rosenthal A., Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=14651934; DOI=10.1016/j.ydbio.2003.08.025;
RA   Kibler K., Svetz J., Nguyen T.-L., Shaw C., Shaulsky G.;
RT   "A cell-adhesion pathway regulates intercellular communication during
RT   Dictyostelium development.";
RL   Dev. Biol. 264:506-521(2003).
RN   [4]
RP   INDUCTION [LARGE SCALE ANALYSIS].
RX   PubMed=18590548; DOI=10.1186/1471-2180-8-109;
RA   Carilla-Latorre S., Calvo-Garrido J., Bloomfield G., Skelton J.,
RA   Kay R.R., Ivens A., Martinez J.L., Escalante R.;
RT   "Dictyostelium transcriptional responses to Pseudomonas aeruginosa:
RT   common and specific effects from PAO1 and PA14 strains.";
RL   BMC Microbiol. 8:109-109(2008).
CC   -!- FUNCTION: Regulates aggregation via a pathway that involves lagC
CC       and tgrD1/lagD. Inhibits lagC and activates lagD expression.
CC       {ECO:0000269|PubMed:14651934}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from early development; required
CC       for aggregation prior to fruiting body formation and sporulation.
CC       {ECO:0000269|PubMed:14651934}.
CC   -!- INDUCTION: Down-regulated by Pseudomonas aeruginosa, PAO1 strain
CC       and up-regulated by PA14 strain infection.
CC       {ECO:0000269|PubMed:18590548}.
CC   -!- DISRUPTION PHENOTYPE: Cells are unable to sporulate when in pure
CC       population although they will sporulate when in chimerae with
CC       wild-type cells. Cells form loose aggregate before disaggregating.
CC       Cells aggregate and disaggregate in waves. comC-/lagC-/tgrD1-
CC       mutant fails to form spores. {ECO:0000269|PubMed:14651934}.
DR   EMBL; AAFI02000006; EAL71536.1; -; Genomic_DNA.
DR   RefSeq; XP_645474.1; XM_640382.1.
DR   ProteinModelPortal; Q55AP8; -.
DR   SMR; Q55AP8; -.
DR   STRING; 44689.DDB0214840; -.
DR   PaxDb; Q55AP8; -.
DR   PRIDE; Q55AP8; -.
DR   EnsemblProtists; EAL71536; EAL71536; DDB_G0271692.
DR   GeneID; 8618102; -.
DR   KEGG; ddi:DDB_G0271692; -.
DR   dictyBase; DDB_G0271692; comC.
DR   eggNOG; KOG1225; Eukaryota.
DR   eggNOG; ENOG410XZMQ; LUCA.
DR   InParanoid; Q55AP8; -.
DR   OMA; CNSSHQG; -.
DR   PhylomeDB; Q55AP8; -.
DR   PRO; PR:Q55AP8; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   Proteomes; UP000002195; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF07974; EGF_2; 3.
DR   SMART; SM00181; EGF; 10.
DR   PROSITE; PS00022; EGF_1; 9.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS50026; EGF_3; 7.
PE   2: Evidence at transcript level;
KW   Complete proteome; Developmental protein; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21   1501       EGF-like domain-containing protein comC.
FT                                /FTId=PRO_0000390620.
FT   TOPO_DOM     21   1446       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1447   1467       Helical. {ECO:0000255}.
FT   TOPO_DOM   1468   1501       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      627    661       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      782    816       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      818    852       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      896    933       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      975   1008       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1043   1077       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1161   1194       EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   CARBOHYD     47     47       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     64     64       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    169    169       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    192    192       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    255    255       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    315    315       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    397    397       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    453    453       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    470    470       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    497    497       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    612    612       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    635    635       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    643    643       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    685    685       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    693    693       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    700    700       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    726    726       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    765    765       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    835    835       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    843    843       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    877    877       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    916    916       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    956    956       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    991    991       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1017   1017       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1122   1122       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1270   1270       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1309   1309       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1334   1334       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1437   1437       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    631    642       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    636    649       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    651    660       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    786    797       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    791    804       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    806    815       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    822    833       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    827    840       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    842    851       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    900    914       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    908    921       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    923    932       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    979    989       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    983    996       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    998   1007       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1047   1058       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1052   1065       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1067   1076       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1165   1175       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1169   1182       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1184   1193       {ECO:0000255|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   1501 AA;  162794 MW;  604D0E17C1A4C062 CRC64;
     MIKKYLFLFF IFLIFNFVLS IQPPLSEYNC LKNFVTKFKL STKFPTNSTG GYDFCSIVSC
     NPVNGSINGF LSLQSESTTP TTVTVVGTDL SCLPFNNLNL QNFLISTTLL YTKFFTSCST
     LAINSDSITS ITQVLAPYET FTIVSKKLNG ALKMSNFINQ KSILITNSNS TSGYTLVNDA
     LAENKIKLET PNFSGLLSVP DLTGYTSLGY PAFYFSDALE VTSLALANIK TIGAVSSRLY
     FPSTKTIQFP TSYHNDTSYL TIQGKFTKPT AVIDLSKFVN CRNIQILNYD KTFNINGEIP
     IKTSPFTDIY YTDGNITKIP IGGTSFVTWS TEQSITIKKS GLSGTLPPLS GVIPTYYDFS
     GNSISGTLSN TWCNTNIIVT DNLMTGTLPS CIVCHLNNSE VAKKFTGNKF TNLVTSNPPC
     TTFAPKIKVD KSQKTIILTG TDFGTYTSGW ILNTTLSCEK LWTKVTYGSN YTCTYPSTTT
     LDKVSYFWIN FNTPGRNYTF PAISQVPTPN SIIVGTSNSV TISGTFFSTY IGYVTQSISV
     GSISCTVGTS SFSSITCTLD SAPSTNTEQK LIITTNSLIK EAYISTVVGF NNNKLCPNDC
     TSSTRGICYM NNGTCKCNSG YVGLDCSGLQ CKVPNCSNGG TCNTTVGLCV CDSSHQSLDC
     SLDFKQCPKG LNSLICSGGG NSCNNQTGIC TCNSSHQGLN CSINYKQCPI GSNSLICSGG
     GNSCNNQTGI CKCDSSHQGS DCANDFIQCP LKNSIPCSGH GICNNKTGDC TCDSGFTNQD
     CSGYTCTSNN CNGHGVCDTS KGICQCYPEW QDIDCQTPFK NCLDPTCSNN GICKNTTGIC
     ECNSSHQGLT CSIDFNQCPI GSNSLICSGG SGNICNNQTG ICTCDSSHQG PDCGTDFIKC
     PTQNLTPCNG FGNCNNITGS CSCDQNHQSE DCNIVYKECP IINSLICNGF DNSCNNQTGV
     CTCDDLHQGL DCGLEYKPCI NNCNGNGVCN NQTSICTCYE AYQGETCQFQ INQCPNNCTT
     GGDCDTITGI CNCYPLRINN DCSGYECLDP NCGDHGICND MNGLCICDKG YRGDNCIYVD
     HYASSVIPTK EEGGTVLIYG LFGEINNDPN VQVGNSNCLI SNITSNSIEC IIGKGSGIKD
     ISVTQNGFEW IGKSMFNYIK SKQSCPNNCN SNGICNDLQG KCECYPGFTG HDCNSLSKTD
     LISPSTPKVN ENTANGIIEN GENKFEIMVI TLQEKTFTNG VLKQYNLENN WKLLEIINDE
     NNNIFKFKQN LTDSSEISIN LEIIKKDRII NFADYSFEIS KDSIKVSINI SNYIYSNSLN
     YLQLHLKSNA YKTNKTSSDD EFDCNLDDGS DAKIDNQDLE NSNINHENFV TIIKDNKILN
     GRYIDHVISD GISTFISSRT IEKDSNSITV GLNLPHCKNC LIDPDFSVLL STDFKENCSD
     SNSNNYIIPV SITVSIGGAA VLVGSAIFFY RKKFIENTLK IQLKRLSKNN SSGSDGGNTQ
     S
//
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