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EMC2_DICDI
ID   EMC2_DICDI              Reviewed;         322 AA.
AC   Q86K48; Q54ZX1;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=ER membrane protein complex subunit 2 {ECO:0000305};
DE   AltName: Full=Tetratricopeptide repeat protein 35;
DE            Short=TPR repeat protein 35;
GN   Name=emc2; Synonyms=ttc35; ORFNames=DDB_G0277149;
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).
CC   -!- FUNCTION: Part of the endoplasmic reticulum membrane protein complex
CC       (EMC) that enables the energy-independent insertion into endoplasmic
CC       reticulum membranes of newly synthesized membrane proteins.
CC       Preferentially accommodates proteins with transmembrane domains that
CC       are weakly hydrophobic or contain destabilizing features such as
CC       charged and aromatic residues. Involved in the cotranslational
CC       insertion of multi-pass membrane proteins in which stop-transfer
CC       membrane-anchor sequences become ER membrane spanning helices. It is
CC       also required for the post-translational insertion of tail-anchored/TA
CC       proteins in endoplasmic reticulum membranes. By mediating the proper
CC       cotranslational insertion of N-terminal transmembrane domains in an N-
CC       exo topology, with translocated N-terminus in the lumen of the ER,
CC       controls the topology of multi-pass membrane proteins. By regulating
CC       the insertion of various proteins in membranes, it is indirectly
CC       involved in many cellular processes. {ECO:0000250|UniProtKB:Q15006}.
CC   -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC       {ECO:0000250|UniProtKB:Q15006}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q15006}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q15006}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q15006}.
CC   -!- SIMILARITY: Belongs to the EMC2 family. {ECO:0000305}.
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DR   EMBL; AAFI02000019; EAL68760.1; -; Genomic_DNA.
DR   RefSeq; XP_642745.1; XM_637653.1.
DR   AlphaFoldDB; Q86K48; -.
DR   SMR; Q86K48; -.
DR   STRING; 44689.DDB0169127; -.
DR   PaxDb; Q86K48; -.
DR   EnsemblProtists; EAL68760; EAL68760; DDB_G0277149.
DR   GeneID; 8621222; -.
DR   KEGG; ddi:DDB_G0277149; -.
DR   dictyBase; DDB_G0277149; -.
DR   eggNOG; KOG3060; Eukaryota.
DR   HOGENOM; CLU_052388_1_0_1; -.
DR   InParanoid; Q86K48; -.
DR   OMA; LMEWAQN; -.
DR   PhylomeDB; Q86K48; -.
DR   PRO; PR:Q86K48; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0072546; C:EMC complex; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0045050; P:protein insertion into ER membrane by stop-transfer membrane-anchor sequence; ISS:UniProtKB.
DR   GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; ISS:UniProtKB.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR039856; EMC2-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR12760; PTHR12760; 1.
DR   Pfam; PF13174; TPR_6; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Repeat; TPR repeat.
FT   CHAIN           1..322
FT                   /note="ER membrane protein complex subunit 2"
FT                   /id="PRO_0000330652"
FT   REPEAT          108..141
FT                   /note="TPR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          143..175
FT                   /note="TPR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          176..209
FT                   /note="TPR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          210..246
FT                   /note="TPR 4"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   322 AA;  37223 MW;  ABBB0C6F33665D19 CRC64;
     MSEMLMLTSS DSIEINRYEE GIRNSGRSFN WVLVRDTLRF LRKSKIRKSN LVSKYGLKLV
     TQYFNKLEDQ EGYDTIEQVI VACLDCGDHT NPKKLFEQLK SKFGKDSVRV QRIHALCLES
     NNQLAEALQI FESILKKYPS DALSMKRQVA IFKGQGNLSK AIQVLNAYLQ IYMCDLEAWL
     ELSSFHISYL SYSTALYCLE EVLLNAPINF VFYIKYAEPL YCLGGNENYN SAVQYYTHAL
     ELNSPTEMDK LDHPPTFLPA IYGIIMSIYS LCEEGYQLKE SQLKLMEWAQ NNLLTITKKY
     SSNDKINLVK HFIDSTDIFN KE
 
 
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