SUN2_DICDI
ID SUN2_DICDI Reviewed; 1278 AA.
AC Q54MI3;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=SUN domain-containing protein 2;
DE Flags: Precursor;
GN Name=sun2; ORFNames=DDB_G0285925;
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).
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: The SUN domain may play a role in nuclear anchoring.
CC {ECO:0000250}.
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DR EMBL; AAFI02000082; EAL64497.1; -; Genomic_DNA.
DR RefSeq; XP_638007.1; XM_632915.1.
DR AlphaFoldDB; Q54MI3; -.
DR SMR; Q54MI3; -.
DR STRING; 44689.DDB0304575; -.
DR PaxDb; Q54MI3; -.
DR EnsemblProtists; EAL64497; EAL64497; DDB_G0285925.
DR GeneID; 8625358; -.
DR KEGG; ddi:DDB_G0285925; -.
DR dictyBase; DDB_G0285925; sunB.
DR eggNOG; KOG1396; Eukaryota.
DR HOGENOM; CLU_263367_0_0_1; -.
DR InParanoid; Q54MI3; -.
DR OMA; PDKFNYA; -.
DR PRO; PR:Q54MI3; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR GO; GO:0005773; C:vacuole; IDA:dictyBase.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR045120; Suco/Slp1-like.
DR InterPro; IPR012919; SUN_dom.
DR PANTHER; PTHR12953; PTHR12953; 1.
DR Pfam; PF07738; Sad1_UNC; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR PROSITE; PS51469; SUN; 1.
PE 3: Inferred from homology;
KW Coiled coil; Glycoprotein; Membrane; Nucleus; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1278
FT /note="SUN domain-containing protein 2"
FT /id="PRO_0000389262"
FT TRANSMEM 914..934
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 501..658
FT /note="SUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00802"
FT REGION 58..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1217..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 177..349
FT /evidence="ECO:0000255"
FT COILED 464..509
FT /evidence="ECO:0000255"
FT COILED 883..914
FT /evidence="ECO:0000255"
FT COMPBIAS 58..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1217..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 832
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 969
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 983
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 994
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 999
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1005
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1028
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1036
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1041
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1049
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1278 AA; 146049 MW; 2F1D31084CDF0FDE CRC64;
MIINKKYILF ILLLLFITSC TIVFSQQQQQ QTEQSEQTEQ AINNDVNNSI NDIFENDSSK
QLRQPQQQHT IVDDGNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN PIDNKDILGL
KKLALLKQFE EQKSKSENDI NNDIVILNLE NDNPNQIIET TTTTLNNSND NKNNIIDDNQ
DEKLNENIKE DKNEIKNEIK NENQEKDKGI IDVEKDENQP NIEEKGKEKQ NLLEKGIENE
NQNENQIQIE KEKEIEIEIE KEKEKENKEL IEESKTEKDN QQKENKENTN EINVTVVEEP
EQPQPQQQNQ QEQQEQQQQE HKEEQQQQEQ QQQEQQTQQE QQTHQQQQEH QETQKNSSEE
TKTQSPIQVN TTDVNNEIEL KNEGDNNSQL NDSSIPITSP LTNDNDTLKT TKEDSNNNNK
NEVINNQTPL IDEKNHQHNY EGNNRNGDDV SIISNIPKTN KAPETQQQQQ QQQQQQQQQQ
QQQQQQQQQQ QQQQQQQQQQ QQQQQQQHVV LTPNDLPDKF NYASSECGAN VLQTNKEAWE
VSSILASSRD RYLLNECNKS QWFVVELCEE IGVQIIELAN FEFFSSMFKD FIVLGSNRYP
AQSWHYLGQF TAENSRKQQY FVLKEKAWYK YLKVKILSHY GDQLYCPISS FKVYGSTMVD
DLKNQVDINI SELEKFQRDL SSIPYPMEIG SDTSYSTTTS TTSSSSTSSS YPSSKTKSSN
SEYPSWERIQ SFSEKLRKNV EQQLIQPPSV LNTNDNNNNN NNNNNNNNNN NNNNNNNNNN
EEQFIYYETN GNGGPPSTST STSSSSSQNH QARTPQSVFK TLADKIKAIE FNQSIGNKFM
EKLERYYSEE IKNLKFDVSE FLNDIIKLGN SLDEKLKDHR KYDDNKFKET SKEIKILKEK
IEKLEEQKSA DRNFYLVVTL VSLLIGLLLK PLFTSSSSSS NKSYPNSMPN SPTYLNSGSN
NYNNNGIINS SGGSGGGGGN LQNSSFIGIN GQLNFSDDNI SAFLNSSCSN FGLNNNNNNN
NGINNNNNNS NSNSNNNSIN NGSININSNN SLQQRIHHNK YIHQRRNSSP LVGVQLESFF
SPNAIPPTIP IVPQDDNNIN YNYNNNNNTN NINNNYNYNN NNNNNNNNNN NNNNNNNNNS
DNYNNNNNSN NNVNSPSSPT PSSIILSPKF ITSIPKNINY YNNGGSGSHL KNRFSRQASE
SVLSQNHYQI NHQNHSLNGV TTNINNNNSN SNGNSNGNSN NMTNGLPPVS MPSSSSHDNL
LLHRGNNQSK KYKRRSHL
