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SIBE_DICDI
ID   SIBE_DICDI              Reviewed;        1946 AA.
AC   Q54JA3;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Integrin beta-like protein E;
DE   Flags: Precursor;
GN   Name=sibE; ORFNames=DDB_G0288239;
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   IDENTIFICATION, AND INTERACTION WITH TALA.
RX   PubMed=16699495; DOI=10.1038/sj.embor.7400701;
RA   Cornillon S., Gebbie L., Benghezal M., Nair P., Keller S.,
RA   Wehrle-Haller B., Charette S.J., Brueckert F., Letourneur F., Cosson P.;
RT   "An adhesion molecule in free-living Dictyostelium amoebae with integrin
RT   beta features.";
RL   EMBO Rep. 7:617-621(2006).
CC   -!- FUNCTION: Implicated in cellular adhesion. {ECO:0000305}.
CC   -!- SUBUNIT: Interacts with talA/talin. {ECO:0000269|PubMed:16699495}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SIB family. {ECO:0000305}.
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DR   EMBL; AAFI02000109; EAL63350.1; -; Genomic_DNA.
DR   RefSeq; XP_636833.1; XM_631741.1.
DR   AlphaFoldDB; Q54JA3; -.
DR   IntAct; Q54JA3; 1.
DR   MINT; Q54JA3; -.
DR   STRING; 44689.DDB0233519; -.
DR   PaxDb; Q54JA3; -.
DR   EnsemblProtists; EAL63350; EAL63350; DDB_G0288239.
DR   GeneID; 8626502; -.
DR   KEGG; ddi:DDB_G0288239; -.
DR   dictyBase; DDB_G0288239; sibE.
DR   HOGENOM; CLU_234725_0_0_1; -.
DR   InParanoid; Q54JA3; -.
DR   PhylomeDB; Q54JA3; -.
DR   PRO; PR:Q54JA3; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..1946
FT                   /note="Integrin beta-like protein E"
FT                   /id="PRO_0000312335"
FT   TOPO_DOM        23..1875
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1876..1896
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1897..1946
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          423..460
FT                   /note="EGF-like"
FT   DOMAIN          514..699
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        203
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        705
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        860
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1043
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1374
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1401
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1513
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1611
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1620
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1662
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1671
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1737
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1743
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1762
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1812
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1852
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1873
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        433..448
FT                   /evidence="ECO:0000250"
FT   DISULFID        450..459
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1946 AA;  206822 MW;  CAA1A41B36BBA0BE CRC64;
     MNNLFKFLFV LLAIFCPPIS DLVVSHGVPQ QHITIIKFTT NFAFRTTFYK TSSSSIVIGE
     KITLGTLTFG DGSSTSVRAS VTSFDTKNDW FFGQFIFTKT YTALTPNNSK QYLAMFTSCC
     RISTLLNNKD ADWNITSSVY LDNKNWPSVN HSPVSGMLPI VQVIANKNNN FRVIASDPNV
     DDKLSFSFST VYPMTQPSGM KINSTGHVFF LPTSVGLYST QIYITDDAVP PAYAVVDFIL
     ESITEPGKCD PSCSNGGATC NGNSECKNCA NAGSTTSNTC STTNYPPYFV SPTPQDNQLI
     PFTVGQPNSI TLSCKSDYTT RTVGIQAANV PAGAAIAEGT SSQGTVKNIL SWTPVAANVG
     VYVTSIFCYD SNGLTSSSRS FTIFIAKPEC GNGHKDPSTG KCKCDGDKWD PTSNCFDCST
     GYYGQNCDPT PPCDKGIPNE GILGDGKCMC INGYSGDKCD VPLSQSCKDL KNSILLSTSV
     PSFFVNPTKV QLYIESDFAL TTSLNIPQKL TKIDVFVLVD VNVASSTLFG VVQSSISTFV
     TEVSKSICET TQFGIGYFSD ASSSGFNFAP GSIIGSNIVN TINGYAVSSY TSTSSGNSLL
     GATNAASNSN GWNSGSFKAI VVLTDKDHSS NSAAITNFVN TYISNSIAPV VVGFGASSIP
     NWNSAISTAD FGYSTVSAAT SIDISAKAVA GLKSVLSNVV YKTDNTTNGA SFVKSTPSDV
     AVSSTADTVK TVSGLVLTKP SATSIVSPVA SVSAIGFGQT DFSINYNRPP TPTGTAFSVN
     QNSFATFKLT GTDPDFNILT FAFTTFLTSD VGVITDSNNK DVSTQKSKYY DSTETFTFTP
     AINYLLPISV SFVANDGCLN STTSATVSIT INKVNQLPTC QQKTISPTLN VANKFVLSAS
     DFEDATPFIQ FTSPTDLTAY GTLTFGGVAV TSTSKIPTSS EITFTQTVNP TNAIDVPVSF
     QAVDSVGAIS TSTCTLTVKL VHTNIKPVSS STSPISVIPR GSVSLTLVST DSDSTSAKFT
     IKSVNKGAKG DFYTCSTNDC TCNSTQTNIY TSISTTTTYT SISYTNKVAN KLICFTNGEP
     SAISNYASIS FTSTDNQGLE SDSVNVVVNI VGNRTNVAPV VTKIQGYSVY QDYLDSDAHV
     VTGTDADIDD YNPPNVNNLI AIITTPPSNG ILVTLQNGSI AATQGKAPFT HYYRPNPGFK
     GTDSYSYQVV DTFKAGSSIE STTVTVNPIN HKPSVVVSSY SFTSQSGDGE TQDLVTSDPD
     GDSVICSVVS IPSQIGMYDS DGNLIESVPT VLSGTSYSFK LLDPSKITPT PFTSVSSSFA
     VKCTDVTTKT IPFGTLSTGV VTANVQYTYI NTPPTTQGGT VQLDQDTVKV FTFNGSDIET
     PKDDIKVKIL SLPINGQLLI NATGVALTTT NIASETYNLN ALSYKPNAGL SNWNTIDQQS
     PLDSISYTVI DQQGLTSDSD IVYFSVRPRN PPVYTGARVI DVLQNTRYPL TITSRIGGGG
     SEVNIQVIGF TNNGTLSIAH NMGSEGTMDS EITSYPNQQS GSTSYNYAYM PPRNKYGNDF
     DFIYFKLFDG DLYSELYTVT VNVIHVNQPP TIELVSYKIL DGVSSEVLFE NTSLINMNIN
     TTVLIKYSGN DIDVDQVTPL ISMIPNFPLR GSLYAYNPTA SNSSGAPITR NSSNVEQNAD
     GFYYVVFVPS KKTSGESYAR ITFIMTDNGG LNSPIVGVLI NVNTVNIAPF VIIGNKNYTT
     QTNLTASVMG VQFDDPDSTT NNVSIVVSIV GQKDDKVASL KDIKLSFTQS PMCEYHQTLA
     SITCIGPKKP LNSSIVSISV IASTAGDYRL KLFVDDLGYN APSAIRAQSH LNATGYVDVK
     VNAPEATTQT TNNKTVLTGA IAGAAAGTAL IAAAAWKLLR KAAPPTDTFF SEAAFLGDGV
     NANPLYEQSA SAAENPLYQS ASDNTD
 
 
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