ID A0A2K5HVM0_COLAP Unreviewed; 975 AA.
AC A0A2K5HVM0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=KASH domain-containing protein {ECO:0000259|PROSITE:PS51049};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000008418.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000008418.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the nesprin family.
CC {ECO:0000256|ARBA:ARBA00008619}.
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 AlphaFoldDB; A0A2K5HVM0; -.
DR Ensembl; ENSCANT00000031233.1; ENSCANP00000008418.1; ENSCANG00000020122.1.
DR Proteomes; UP000233080; Unplaced.
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; IPR026696; AKAP6/CEP68.
DR InterPro; IPR012315; KASH.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR14514:SF3; NESPRIN-1; 1.
DR PANTHER; PTHR14514; PKA ANCHORING PROTEIN; 1.
DR Pfam; PF10541; KASH; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM01249; KASH; 1.
DR SMART; SM00150; SPEC; 4.
DR SUPFAM; SSF46966; Spectrin repeat; 4.
DR PROSITE; PS51049; KASH; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00385}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00385}; Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT TOPO_DOM 1..924
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00385"
FT TOPO_DOM 946..975
FT /note="Perinuclear space"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00385"
FT DOMAIN 916..975
FT /note="KASH"
FT /evidence="ECO:0000259|PROSITE:PS51049"
FT REGION 401..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 975 AA; 111394 MW; 874E86EBA15207A6 CRC64;
MVVAEDLRAL RMAEDGCVDA DLPDCNCDVT RVKKLKETLV AVQQLDKNMS SLRTWLAHIE
SELAKPIVYD SCNSEEIQRK LNEQQELQRD IEKHSTGVAS VLNLCEVLLH DCDACATDAE
CDSIQQATRN LDRRWRNICA MSMERRLKIE ETWRLWQKFL DDYSRFEDWL KTSERTAAFP
SSSGVIYTVA KEELKKFEAF QRQVHECLTQ LELINKQYRR LARENRTDSA CSLKQMVHEG
NQRWDNLQKR VTSILRRLKH FIGQREEFET ARDSILVWLT EMDLQLTNIE HFSECDVQAK
IKQLKAFQQE ISLNHNKIEQ IIAQGEQLIE KSEPLDAAII EEELDELRRY CQEVFGRVER
YHKKLISLPL PDDEHDLSDR ELELEDSAAL SDLHWHDRSA DSLLSPQPSS NPSLSLAQPL
RSERSGRDTP ASVDSIPLEW DHDYDLSRDL ESAVSRALPS EDEESQDDKD FYLRGAVGLS
DVMIPESPEA YVKLTENAIK NTSGDHSALE SQIRQLGKAL DDSRFQIQQT ENIIRSKTPT
GPELDTSYKG YMKLLGECSG SIDSVKRLEH KLKEEEESLP GFVNLHSTET QTAGVIDRWE
LLQAQALSKE LRMKQNLQKW QQFNSDLNSI WAWLGDTEEE LEQLQRLELS TDIQTIELQI
KKLKELQKAV DHRKAIILSI NLCSPEFTQA DSKESRDLQD RLSQMNGRWD RVCSLLEEWR
GLLQDALMQC QGFHEMSHGL LLMLENIDRR KNEIVPIDSN LDAEILQDHH KQLMQIKHEL
LESQLRVASL QDMSCQLLVN AEGTDCLEAK EKVHVIGNRL KLLLKEVSRH IKELEKLLDV
SSSQQDLSSW SSADELDTSG SVSPTSGRST PNRQKTPRGK CSLSQPGPSV SSPHSRSTKG
GSDSSLSEPG PDRSGRAFLF RVLRAALPLQ LLLLLLIGLA CLVPMSEEDY SCALSNNFAR
SFHPMLRYTN GPPPL
//
