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LIMCH_DICDI
ID   LIMCH_DICDI             Reviewed;         686 AA.
AC   Q55GV9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Calponin homology and LIM domain-containing protein;
DE            Short=CH-LIM;
GN   Name=ChLim; ORFNames=DDB_G0267490;
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=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   [2]
RP   FUNCTION, INDUCTION, AND INTERACTION WITH LIMF AND RAB21.
RX   PubMed=15962002; DOI=10.1038/sj.emboj.7600716;
RA   Khurana T., Brzostowski J.A., Kimmel A.R.;
RT   "A Rab21/LIM-only/CH-LIM complex regulates phagocytosis via both activating
RT   and inhibitory mechanisms.";
RL   EMBO J. 24:2254-2264(2005).
CC   -!- FUNCTION: Involved in the regulation of phagocytosis. May repress
CC       rab21. {ECO:0000269|PubMed:15962002}.
CC   -!- SUBUNIT: Interacts with limF and rab21. {ECO:0000269|PubMed:15962002}.
CC   -!- INTERACTION:
CC       Q55GV9; Q86I44: limF; NbExp=3; IntAct=EBI-1808948, EBI-1808928;
CC   -!- INDUCTION: Repressed by limF. {ECO:0000269|PubMed:15962002}.
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DR   EMBL; AAFI02000003; EAL73198.1; -; Genomic_DNA.
DR   RefSeq; XP_647075.1; XM_641983.1.
DR   AlphaFoldDB; Q55GV9; -.
DR   SMR; Q55GV9; -.
DR   IntAct; Q55GV9; 2.
DR   STRING; 44689.DDB0231986; -.
DR   PaxDb; Q55GV9; -.
DR   EnsemblProtists; EAL73198; EAL73198; DDB_G0267490.
DR   GeneID; 8615879; -.
DR   KEGG; ddi:DDB_G0267490; -.
DR   dictyBase; DDB_G0267490; ChLim.
DR   eggNOG; KOG1703; Eukaryota.
DR   eggNOG; KOG1704; Eukaryota.
DR   HOGENOM; CLU_401396_0_0_1; -.
DR   InParanoid; Q55GV9; -.
DR   OMA; CEVISYV; -.
DR   Reactome; R-DDI-6798695; Neutrophil degranulation.
DR   PRO; PR:Q55GV9; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:dictyBase.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR   GO; GO:0001891; C:phagocytic cup; IDA:dictyBase.
DR   GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR   GO; GO:0008270; F:zinc ion binding; ISS:dictyBase.
DR   GO; GO:0046847; P:filopodium assembly; IMP:dictyBase.
DR   GO; GO:0050765; P:negative regulation of phagocytosis; IMP:dictyBase.
DR   GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR   CDD; cd00014; CH; 1.
DR   Gene3D; 1.10.418.10; -; 1.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR037987; FHL2/3/5.
DR   InterPro; IPR003096; SM22_calponin.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR24205; PTHR24205; 3.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF00412; LIM; 4.
DR   PRINTS; PR00888; SM22CALPONIN.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00132; LIM; 6.
DR   SUPFAM; SSF47576; SSF47576; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 3.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 6.
PE   1: Evidence at protein level;
KW   LIM domain; Metal-binding; Phagocytosis; Reference proteome; Repeat; Zinc.
FT   CHAIN           1..686
FT                   /note="Calponin homology and LIM domain-containing protein"
FT                   /id="PRO_0000328170"
FT   DOMAIN          15..120
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          139..200
FT                   /note="LIM zinc-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          219..279
FT                   /note="LIM zinc-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          373..435
FT                   /note="LIM zinc-binding 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          437..495
FT                   /note="LIM zinc-binding 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          519..579
FT                   /note="LIM zinc-binding 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          583..658
FT                   /note="LIM zinc-binding 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   REGION          305..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..339
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   686 AA;  76480 MW;  0EFAAD648D5D5AEC CRC64;
     MIKANWTSTS AFNLELALDE SRDWIERVIN QKFPSDFQSS LRDGIFLCKL INQIQPNSVP
     KYNQSPSTDF AKRENIQLFI KSAKHSMGLR DTQLFESQDL FESIRIRNIA ITLYWLGRAA
     RASQTYKGPQ LDLLKFQGMN CSACKKAITN NDYLTTMTQQ FHTSCAVCCS CSCKLDPKKK
     FYQESNNFWC ENCMLGATNL GGSNNSSGGK NKSNNNNNNK CSGCFGSLEK GYVPDENDKE
     KKYCTSCICD LCHDPLIGNF QVKDGKKVCD SCSCKSCGKS LEDGYYEEGI SKYCEPCAKD
     RNKPKQVMDK DGHDHHHHNH NKPTTTTTTT NSNSPLAKKK SDSCKMCDKP VDNKTKKYGD
     DRDKYCTPHE KDGTCGKCNG ELVGSAISVM DKNFHPQCFK CDSCNKNLNQ NDQIKKSPTT
     GNPLCGPCSS NNNKSSKNCH DCKKPISGSS VEALDRPYHP NCLKCYSCSK NLKEDFTEVD
     NEPFCNPCAS QLNQYTSGNQ KQPKQGGSPF ITSGWLDSDR CVVCVKPLNG EVAKIFDSFY
     HKGCFKCTDK SCNAPLLTGY FPHDKKPYCQ KCSIKIQQST TTDHCAKCSK PIIEGSILKV
     AGKVYHKSCY DNEKHTSSSS SSSSVNCFKC KSQITGTQFV RLDQKDYCMK CSPSASSSTT
     VTHGERLNYG MTVDPRSGKR VFNTSK
 
 
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