SADA_DICDI
ID SADA_DICDI Reviewed; 952 AA.
AC Q8I7T3; Q54IT9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Substrate-adhesion molecule;
DE Flags: Precursor;
GN Name=sadA; ORFNames=DDB_G0288511;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=AX3;
RX PubMed=12499361; DOI=10.1083/jcb.200206067;
RA Fey P., Stephens S., Titus M.A., Chisholm R.L.;
RT "SadA, a novel adhesion receptor in Dictyostelium.";
RL J. Cell Biol. 159:1109-1119(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: Involved in substrate adhesion, myosin-independent
CC cytokinesis, organization of actin cytoskeleton, and phagocytosis.
CC {ECO:0000269|PubMed:12499361}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed during vegetative growth, but not in
CC developing cells.
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DR EMBL; AY178767; AAO13155.1; -; Genomic_DNA.
DR EMBL; AAFI02000114; EAL63177.1; -; Genomic_DNA.
DR RefSeq; XP_636687.1; XM_631595.1.
DR AlphaFoldDB; Q8I7T3; -.
DR STRING; 44689.DDB0191090; -.
DR PaxDb; Q8I7T3; -.
DR EnsemblProtists; EAL63177; EAL63177; DDB_G0288511.
DR GeneID; 8626671; -.
DR KEGG; ddi:DDB_G0288511; -.
DR dictyBase; DDB_G0288511; sadA.
DR eggNOG; KOG1225; Eukaryota.
DR HOGENOM; CLU_309604_0_0_1; -.
DR InParanoid; Q8I7T3; -.
DR OMA; FIKRFIM; -.
DR PRO; PR:Q8I7T3; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:dictyBase.
DR GO; GO:0000902; P:cell morphogenesis; IMP:dictyBase.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0034394; P:protein localization to cell surface; IMP:dictyBase.
DR GO; GO:0050821; P:protein stabilization; IMP:dictyBase.
DR CDD; cd00055; EGF_Lam; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR002049; LE_dom.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS50026; EGF_3; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Phagocytosis; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..952
FT /note="Substrate-adhesion molecule"
FT /id="PRO_5000089299"
FT TOPO_DOM 26..527
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..591
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 592..612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 613..678
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 700..722
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 723..743
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 744..752
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 753..773
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 774..801
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 802..822
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 823..837
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 838..858
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 859..868
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 869..889
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 890..897
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 898..918
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 919..952
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 438..471
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 442..452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 446..459
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 461..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 952 AA; 104675 MW; 3DFA579C16DB3696 CRC64;
MKSQKIGSMI LLIGILLAIF NFAYSDDDIE RFSINPEKPI SFTSDQPGFP TSADFPIGSI
LANSFYSFGG DVNYFQLNIS LMEEFSKDGN TGSQATWNQY TSVPVSPISS AVTANRVYTM
SIGSLNRVKK GDITSMESTD FLNDEKYSSL VTTLNGGVSY GDDVFFLSSK SATGEAVLIH
INDTATGTFG TSSYDEILLD AAINDPSSIT VDSKLGLAFI GDSDGDILVF NMTLKAKIAI
YSNSSIANLR SSGVVDEERQ LLYICGQAGG MNSYITQVDI FHYSATDITL LHSFTILGSL
CPSAGIDVKG GQLFFSTTTS SGSQLIGTDT SGGNTGSLSE NIANTQSVAI SVDSITKTIS
VFYPDSVFYG TFKSICPSDC SGHGECNYGT CVCDHNYQGQ GCEEELCLTL NNCTGTDNGK
CENGFCYCSS EWEGAQCEIR RCKDSCNGYG TCNTANYTCV CDSAHMGETC NELVPPPPCT
YYTDSESCLS RTTCGWCEVD GLCKEGDRYG PFEGFCRTWF FDTNVETGVI ALACIFIAFV
GILYIIDIGT TVPIDIKRAK DYAEENKSGQ FPKATHEEAS VLWWRDQRSH KAWTFMDQFQ
LISLVSHIGV VFPSRFISFT EYLDWSNLGI PLPPSINPPQ IWSVPTDWTS NTARTILSMA
QYENSLGSGD LYLLPNILFW FGLLLGVFLV PLLLAYAIIS FMESLIHWKE VVTNRLIHVL
VRILTFGYIG VLIAASFAMV TPLHDYRIII PGAIIFVLYG IGLPIAIWFL LAVPEARLHN
PTFKQRFGCL YVHYKPKTDH RFVVFMFIKR FIMAVIIGIL SFKPMTNYPL TGTDLAVPIV
QVVVIDIALI GYAVLLFIRK PYFDHYQLWL EYLLTAINIV TVSLSLTHIK SPSAAGELIA
CLIQALALVA CIAAYVVAWL QMRSSFIKKV KKYLCCCCKS SKSSGEIDLS KK
