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Database: UniProt
Entry: A0A3L8SX35_CHLGU
LinkDB: A0A3L8SX35_CHLGU
Original site: A0A3L8SX35_CHLGU 
ID   A0A3L8SX35_CHLGU        Unreviewed;       909 AA.
AC   A0A3L8SX35;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=KASH domain-containing protein {ECO:0000259|PROSITE:PS51049};
GN   ORFNames=DV515_00001878 {ECO:0000313|EMBL:RLW10416.1};
OS   Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC   Chloebia.
OX   NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW10416.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLW10416.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLW10416.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLW10416.1};
RX   PubMed=30282656;
RA   Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA   Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT   "A non-coding region near Follistatin controls head colour polymorphism in
RT   the Gouldian finch.";
RL   Proc. R. Soc. B 285:0-0(2018).
CC   -!- SIMILARITY: Belongs to the nesprin family.
CC       {ECO:0000256|ARBA:ARBA00008619}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLW10416.1}.
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DR   EMBL; QUSF01000004; RLW10416.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L8SX35; -.
DR   Proteomes; UP000276834; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005635; C:nuclear envelope; IEA:UniProt.
DR   CDD; cd00176; SPEC; 3.
DR   Gene3D; 1.20.58.60; -; 4.
DR   InterPro; IPR039906; Anc-1/SYNE1/2-like.
DR   InterPro; IPR012315; KASH.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   PANTHER; PTHR21524; SPECTRIN REPEAT CONTAINING NUCLEAR ENVELOPE PROTEIN 2; 1.
DR   PANTHER; PTHR21524:SF6; SPECTRIN REPEAT-CONTAINING NUCLEAR ENVELOPE PROTEIN 2; 1.
DR   Pfam; PF10541; KASH; 1.
DR   Pfam; PF00435; Spectrin; 3.
DR   SMART; SM01249; KASH; 1.
DR   SMART; SM00150; SPEC; 5.
DR   SUPFAM; SSF46966; Spectrin repeat; 4.
DR   PROSITE; PS51049; KASH; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU00385}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00385}; Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   TOPO_DOM        1..858
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00385"
FT   TOPO_DOM        880..909
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00385"
FT   DOMAIN          850..909
FT                   /note="KASH"
FT                   /evidence="ECO:0000259|PROSITE:PS51049"
FT   REGION          363..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          808..843
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          719..748
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        378..392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..523
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        827..843
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   909 AA;  104705 MW;  4A54817EBB9E6268 CRC64;
     MPAWSPRRFP PRSLGSAGRG MVLPCGPVKK LKETFTFIQL LDKNMSNLRT WLARIESELS
     KPVVYDICDD QEIQKRLAEQ QDLQRDIEQH TAGVESVFNI CDVLLHDSDA CANETECDSI
     QQTTRSLDRR WRNICAMSME RRMKIEETWR LWQRFLDDYS RFEDWLKASE NIAARPNSSE
     VLYTHAKEEL KKFEAFQRQI HERLTQLELI NKQYRRLARE NRTDSASKLK QMVHEGNQRW
     DNLQKRVASI LRRLKHFTNR RDEFEGTRES ILVWLTEMDL QLTNVEHFSK SNFDDKMRQL
     NGFQQEITLN TNKIDQLIVF GEQLIQKSEP LDAILIEDEL EELHRYCQEV FGRVARFHQR
     LTSRDPGLDD EKDNSENETD QEDSREIQND PWHKKAIAEG PSSAQSLCHL MPPTQGHERS
     GCETPVSVDS IPLEWDHTGD VGGSSSHEDD EEATYYSALS GKSVSEAHPW HSPGSPVCRK
     HRYNQAEMVG NVLSGPETST PYKPEYVKQL SSASSSSGKE KIPSATMSDE EPQDDQELVN
     IAAAEKQSGI IDRWELIQAQ DLRNKLRMKQ KLQQWQQLDS DLSDISAWLD KTEQELEELQ
     KVKLPTSMQA LEQKVKKLKD MLKAFDSYKA VLLSANLSSK EFQKADSTEF KELQNRLRKV
     NLHWEKATRA LDNWRKGLQQ ALLQCQDFHD QSQKLILWLA SAESRRSEAQ ITAPNADLNA
     ILECQKELMQ LEKELLEQQL NVNSLQELTA YLLLKSDGDY IEEEEKVHVI GTKLKQLIEQ
     VSHDLKTIQG NLDAKTFLLV PDDLDSGVYN PEEEKSSPAM ALRRTADGRN GSSTRSESHS
     QAVQANPRSP SFFYRVLRAA LPLQLFFLLL LLLACMIPSS EEDYSCSQAN NFARSFYPML
     RYTNGPPPT
//
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