COMC_DICDI
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 25-MAY-2022, entry version 87.
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; Evosea; Eumycetozoa; Dictyostelia; 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., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA 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., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., 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., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., 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., Kay R.R.,
RA Ivens A., Martinez J.L., Escalante R.;
RT "Dictyostelium transcriptional responses to Pseudomonas aeruginosa: common
RT 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 and
CC 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 for
CC aggregation prior to fruiting body formation and sporulation.
CC {ECO:0000269|PubMed:14651934}.
CC -!- INDUCTION: Down-regulated by Pseudomonas aeruginosa, PAO1 strain and
CC up-regulated by PA14 strain infection. {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 wild-type
CC cells. Cells form loose aggregate before disaggregating. Cells
CC aggregate and disaggregate in waves. comC-/lagC-/tgrD1-mutant fails to
CC form spores. {ECO:0000269|PubMed:14651934}.
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DR EMBL; AAFI02000006; EAL71536.1; -; Genomic_DNA.
DR RefSeq; XP_645474.1; XM_640382.1.
DR AlphaFoldDB; Q55AP8; -.
DR STRING; 44689.DDB0214840; -.
DR PaxDb; 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 HOGENOM; CLU_003793_0_0_1; -.
DR InParanoid; Q55AP8; -.
DR OMA; CTTFAPK; -.
DR PhylomeDB; Q55AP8; -.
DR PRO; PR:Q55AP8; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
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 Developmental protein; Disulfide bond; EGF-like domain; Glycoprotein;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1501
FT /note="EGF-like domain-containing protein comC"
FT /id="PRO_0000390620"
FT TOPO_DOM 21..1446
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1447..1467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1468..1501
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 627..661
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 782..816
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 818..852
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 896..933
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 975..1008
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1043..1077
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1161..1194
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 693
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 700
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 726
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 835
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 843
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 877
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 916
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 956
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 991
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1017
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 631..642
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 636..649
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 651..660
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 786..797
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 791..804
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 806..815
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 822..833
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 827..840
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 842..851
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 900..914
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 908..921
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 923..932
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 979..989
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 983..996
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 998..1007
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1047..1058
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1052..1065
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1067..1076
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1165..1175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1169..1182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1184..1193
FT /evidence="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
