SIBC_DICDI
ID SIBC_DICDI Reviewed; 1954 AA.
AC Q54JA5;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Integrin beta-like protein C;
DE Flags: Precursor;
GN Name=sibC; ORFNames=DDB_G0288195;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000109; EAL63328.1; -; Genomic_DNA.
DR RefSeq; XP_636831.1; XM_631739.1.
DR AlphaFoldDB; Q54JA5; -.
DR IntAct; Q54JA5; 1.
DR MINT; Q54JA5; -.
DR STRING; 44689.DDB0233526; -.
DR PaxDb; Q54JA5; -.
DR ABCD; Q54JA5; 2 sequenced antibodies.
DR EnsemblProtists; EAL63328; EAL63328; DDB_G0288195.
DR GeneID; 8626500; -.
DR KEGG; ddi:DDB_G0288195; -.
DR dictyBase; DDB_G0288195; sibC.
DR eggNOG; ENOG502R9GV; Eukaryota.
DR HOGENOM; CLU_234725_0_0_1; -.
DR InParanoid; Q54JA5; -.
DR OMA; YIVVDFI; -.
DR PhylomeDB; Q54JA5; -.
DR PRO; PR:Q54JA5; -.
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 GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
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; PS50026; EGF_3; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1954
FT /note="Integrin beta-like protein C"
FT /id="PRO_0000312333"
FT TOPO_DOM 21..1883
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1884..1904
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1905..1954
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 428..465
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 521..706
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1678
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1742
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1770
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1860
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1881
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 438..453
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 455..464
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1954 AA; 208451 MW; 979CA9CC790AA864 CRC64;
MNKLFYLFIL IASLFILTDA SHFRFGTISW QPTTDYRTIK FTSNFAYRTT FFYSSTSSIK
VGNLVNVGTL NFGSGVGSVT VSVTVTDFDV KNNWFTGTFT TTKAYPAQNS GTIREYTAIF
TSCCRISSLL NNKDASWNIT TSVQIDNKNE LSMVNWSPVS GMIPIVQVVA NKNNNFRVIA
SDQNVQNADS SALTFSFSKV YTMTQPSGMT IDSKGNCYFL PTQIGLYSTQ IYILDSRGAY
IVVDFILQSV AEPGTCDPTC SNAGTACNQN SQCKGCTNSG STTIDTCTTS NYPPDFVSPP
TPDDGDTKLF PIGASTSLTF SCKTIMSGRS TTIQTANLPV GVTTKTPVTG ATSNTTITWT
PTTANTGSYV VSLVCSDSTG LTSSVRSFTI LVAKPDCGNG GYTESGVCKC VDNWDPASKC
FECKDGYYGE NCVAVPPCVN GVPNSGINGD GKCLCSNGWT GADCSISSSQ SCKDLSNSNT
SISYSNPSFV NPTKVQVYLT STPNYEVPTI VSIPNPINNL DVYVLVDANL ASTTAFGYIK
SGMSTFVSNI ENICETAQFG IGYFSDYTPS PISFSPSQVM GSPIAAAIGL YKPATYSTTS
NGNSLLAATD AASASVGWNS GSFKVIVIIT DSDHSSSSAQ ITAFTNKFIG KSIVPVVVSF
GASSMTNWNS ALTSAGFGSV VTASGTSASD WSAKANTGVK NVLSKIVYKS DPTATGSSFV
SSVPSTVTVS SSSSTQQTVN GLKLSLPSGT TIVSPVATIS AMGYGQTDIS INYNRPPVAT
SGSFSVNQNS LATFKLTGTD PDANILQFKF TTFLTANAGV ITDSNGKDVS KQQSNYYAAS
EIFTYTPFEN YLASNTIRFV AFDGCVESNT YATISITINK VNQLPECSSI SSTITTTLNT
QSTFSMTATD FEDASPFLQF TKPTDLTAYG TFTYKGASIT SSTKITTGDS VIFTQTVNPK
NDATVTLEFR AIDTSNAFSQ ASCSVSFKIQ HANVAPVSSS TSPISVIPRG SVSLTLVSTD
SDSTKALFTI TAIKNGNNGN FYTCSTNDCS CTSGSSDSTI ISLKDQFSGI SYSSTKANKL
ICFTNGEPSA ISNYASISFT STDDEGLESN TVSVVVNIVG DRANVAPVVT KIQDYSVYQD
YLDSDAHVVT GTDADIDDYN PPNVNNLIAI ITTPPSNGIL VTVQNGNNVA TQGNAPFTHY
YRPNPGFKGT DSYSYQVMDT FKETSSVEST TVTVNPINHK PTLTVNSYSF TSQSGAGETQ
TLVTYDFDGD NVLCSVQAAP KQISMYDSEN ELITTLPKSL SSNSYSFKLL DASKISPTPF
SSFSDSFIIS CKDDSKLTTP YGVLSTGNVT GFVQFTYINT PPTTKGIQVE LDQDTTEPFT
FNGTDIESPS DLKAKIYALP ANGQLLNGNV VLTSKLIGEE TYELDALSYK PNAGLSNWNT
IDNIGPLDSI PYSVVDQQGL VSDSDVVTFS VRPRNPPVYT GADVIDVLQN TRYPLNVQGK
VGNGGSEVNI QVLKFSGRGT LSIAHSMGSE GTMDTEITSY PNSQTGSTSY NFAYMPPHNE
YGNDFDFIEF KLFDGDLYSE LYTITVNVIH VNQPPTIQLI SYKVLDDTSK DNGEVLFDST
YIVNMNINTS VLIKYTGSDV DVDQVTPLLS TVTTALRGTL YTKDETVPDL KGSIIDRNHT
TVEQSSDGYY YVVYSPVPDS SGNSYVRIPF FMTDNGGLDS PTLTAVINVN RYNIPPFVLA
GNKTYSTTTK LALSVENVQF DDPDSGKSNN VSIVVSIVGE NDENVASLED IKISLKRMQN
CELHTSLASI SCLDTKSALN ESIQTITVNA VTAGNYRLKL FVDDLGYNAP SAIRAQSHMN
ATGYVDVTFE EAETTTQTND NKTVLTGAIA GAAAGTALIA AAAWRLLRKA APPTDTFFSE
AAFLGDGVSS NPLYEQSASA AENPLYQSAS DTTD
