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COMI_DICDI
ID   COMI_DICDI              Reviewed;         185 AA.
AC   Q03380; Q54HA3;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=Comitin;
DE   AltName: Full=24 kDa actin-binding protein;
DE   AltName: Full=CABP1-related protein p24;
GN   Name=comA; Synonyms=capA, capC; ORFNames=DDB_G0289599;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 101-113.
RC   STRAIN=AX2;
RX   PubMed=2114316; DOI=10.1016/0014-5793(90)81521-o;
RA   Noegel A.A., Gerisch G., Lottspeich F., Schleicher M.;
RT   "A protein with homology to the C-terminal repeat sequence of Octopus
RT   rhodopsin and synaptophysin is a member of a multigene family in
RT   Dictyostelium discoideum.";
RL   FEBS Lett. 266:118-122(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=V12M2;
RX   PubMed=1338410; DOI=10.1139/o92-149;
RA   Greenwood M.T., Tsang A.;
RT   "Regulation of the gene encoding the p24 actin-binding protein in
RT   Dictyostelium discoideum.";
RL   Biochem. Cell Biol. 70:1047-1054(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Schreiner T., Noegel A.A.;
RT   "The vesicle- and actin-associated protein comitin has a role in
RT   phagocytosis and in protection against osmotic stress.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   CHARACTERIZATION.
RX   PubMed=8635456; DOI=10.1002/j.1460-2075.1996.tb00465.x;
RA   Jung E., Fucini P., Stewart M., Noegel A.A., Schleicher M.;
RT   "Linking microfilaments to intracellular membranes: the actin-binding and
RT   vesicle-associated protein comitin exhibits a mannose-specific lectin
RT   activity.";
RL   EMBO J. 15:1238-1246(1996).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=AX2;
RX   PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA   Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA   Soldati T.;
RT   "Proteomics fingerprinting of phagosome maturation and evidence for the
RT   role of a Galpha during uptake.";
RL   Mol. Cell. Proteomics 5:2228-2243(2006).
CC   -!- FUNCTION: May have a role in cell motility. It has high affinity for
CC       both G-actin and F-actin. Binds to vesicle membranes via mannose
CC       residues and, by way of its interaction with actin, links these
CC       membranes to the cytoskeleton.
CC   -!- SUBUNIT: Homodimer in solution.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane
CC       protein. Endomembrane system; Peripheral membrane protein. Cytoplasm,
CC       cytoskeleton. Note=Primarily on Golgi and vesicle membranes.
CC   -!- DEVELOPMENTAL STAGE: Levels of p24 mRNA increase rapidly during early
CC       development and then drop sharply after aggregation.
CC   -!- PTM: The N-terminus is blocked.
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DR   EMBL; X54016; CAA37963.1; -; mRNA.
DR   EMBL; X54062; CAA37997.1; -; mRNA.
DR   EMBL; AY007806; AAG32535.1; -; Genomic_DNA.
DR   EMBL; AAFI02000147; EAL62617.1; -; Genomic_DNA.
DR   PIR; S10711; S21366.
DR   RefSeq; XP_636121.1; XM_631029.1.
DR   AlphaFoldDB; Q03380; -.
DR   SMR; Q03380; -.
DR   STRING; 44689.DDB0219923; -.
DR   PaxDb; Q03380; -.
DR   EnsemblProtists; EAL62617; EAL62617; DDB_G0289599.
DR   GeneID; 8627224; -.
DR   KEGG; ddi:DDB_G0289599; -.
DR   dictyBase; DDB_G0289599; comA.
DR   eggNOG; ENOG502RSSN; Eukaryota.
DR   HOGENOM; CLU_1463829_0_0_1; -.
DR   InParanoid; Q03380; -.
DR   OMA; SAIWASG; -.
DR   PhylomeDB; Q03380; -.
DR   PRO; PR:Q03380; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005911; C:cell-cell junction; IDA:dictyBase.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005768; C:endosome; IDA:dictyBase.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:dictyBase.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030660; C:Golgi-associated vesicle membrane; IDA:dictyBase.
DR   GO; GO:0005811; C:lipid droplet; HDA:dictyBase.
DR   GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR   GO; GO:0030867; C:rough endoplasmic reticulum membrane; IDA:dictyBase.
DR   GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR   GO; GO:0003785; F:actin monomer binding; IDA:dictyBase.
DR   GO; GO:0042802; F:identical protein binding; IPI:dictyBase.
DR   GO; GO:0005537; F:mannose binding; NAS:dictyBase.
DR   GO; GO:0051017; P:actin filament bundle assembly; IDA:dictyBase.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:dictyBase.
DR   GO; GO:0006972; P:hyperosmotic response; IMP:dictyBase.
DR   GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR   GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
DR   GO; GO:0051591; P:response to cAMP; IDA:dictyBase.
DR   GO; GO:0046898; P:response to cycloheximide; IDA:dictyBase.
DR   GO; GO:0051707; P:response to other organism; TAS:dictyBase.
DR   CDD; cd00028; B_lectin; 1.
DR   Gene3D; 2.90.10.10; -; 2.
DR   InterPro; IPR001480; Bulb-type_lectin_dom.
DR   InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR   SMART; SM00108; B_lectin; 1.
DR   SUPFAM; SSF51110; SSF51110; 1.
DR   PROSITE; PS50927; BULB_LECTIN; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Golgi apparatus; Lectin; Membrane; Reference proteome; Repeat.
FT   CHAIN           1..185
FT                   /note="Comitin"
FT                   /id="PRO_0000206367"
FT   DOMAIN          1..123
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   REPEAT          153..158
FT                   /note="2-1"
FT   REPEAT          159..164
FT                   /note="2-2"
FT   REPEAT          165..170
FT                   /note="2-3"
FT   REPEAT          171..176
FT                   /note="2-4"
FT   REPEAT          177..182
FT                   /note="2-5"
FT   REGION          138..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..182
FT                   /note="5 X 6 AA tandem repeats of G-Y-P-X-Q-[PH]"
FT   COMPBIAS        151..175
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   185 AA;  20697 MW;  CEEF5912398E4FFD CRC64;
     MELLRQGEHL HSTSRSTLES KCRKYKLIMQ NDGNLVLYIG SLKSQSDEYC LWSSASCGKG
     HGPYRLSMQE DGNLVIYDSR NSAIWASGTM GHGVRGHYSM KLRSSGQIVV YDKYKQILYS
     SKPCTRDHLL SLPCAKPSGH PQSAYPPQQP GYGYPAQPGY PPQPGYPPQH GYPPQHGYPQ
     QPGYY
 
 
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