ID A0A8B8EKL0_CRAVI Unreviewed; 1301 AA.
AC A0A8B8EKL0;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE SubName: Full=CAP-Gly domain-containing linker protein 1-like isoform X24 {ECO:0000313|RefSeq:XP_022340705.1};
GN Name=LOC111135171 {ECO:0000313|RefSeq:XP_022340705.1};
OS Crassostrea virginica (Eastern oyster).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX NCBI_TaxID=6565 {ECO:0000313|Proteomes:UP000694844, ECO:0000313|RefSeq:XP_022340705.1};
RN [1] {ECO:0000313|RefSeq:XP_022340705.1}
RP IDENTIFICATION.
RC TISSUE=Whole sample {ECO:0000313|RefSeq:XP_022340705.1};
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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 RefSeq; XP_022340705.1; XM_022484997.1.
DR GeneID; 111135171; -.
DR OrthoDB; 2130750at2759; -.
DR Proteomes; UP000694844; Chromosome 5.
DR GO; GO:0005938; C:cell cortex; IEA:TreeGrafter.
DR GO; GO:0035371; C:microtubule plus-end; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0051010; F:microtubule plus-end binding; IEA:TreeGrafter.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:TreeGrafter.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 2.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR032108; CLIP1_ZNF.
DR PANTHER; PTHR18916:SF82; CAP-GLY DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR18916; DYNACTIN 1-RELATED MICROTUBULE-BINDING; 1.
DR Pfam; PF01302; CAP_GLY; 2.
DR Pfam; PF16641; CLIP1_ZNF; 1.
DR SMART; SM01052; CAP_GLY; 2.
DR SUPFAM; SSF74924; Cap-Gly domain; 2.
DR SUPFAM; SSF90257; Myosin rod fragments; 1.
DR PROSITE; PS00845; CAP_GLY_1; 2.
DR PROSITE; PS50245; CAP_GLY_2; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Reference proteome {ECO:0000313|Proteomes:UP000694844}.
FT DOMAIN 104..146
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 245..287
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 359..548
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 151..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..209
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..352
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1301 AA; 145647 MW; C1E1053912E7D06D CRC64;
MSLPRPSGLK APTKIGRPTG LPQPRSAGTG IPTPGSVHKA QSAIAKSARA AGISAHLAEK
YAAEMVQKLP GPDSLPPPPP ADDFIIGDRV WVSGTKPGHI SYIGETKFAA GEWAGVVLDN
AEGKNDGSVQ GVRYFQCEPK RGVFSRISKL SRTPGISSET PKPEDCVSES GGSISVKANG
TTHLPSSLRP TTPKPISASR ALSTSSSSLN KAGIASTPTA KKPSLKIGDR VLVSGTKTGT
LRYIGATDFA KGDWAGVELD EKQGKNDGAV SGKRYFECRP MFGLFAPVHK VTRLTSGNIT
NSMSASTPSP QSRSLMNTSL RLSRERSGSQ DSVSSISSTA SSVSRSRAKT SQRPSSLNLT
ATTQALQKAL KEKEEHIEQL LKERDLERAE VARAAAQVDE AEGQLANMRS EQDRFREDTD
EAITRLRTRV EELEKERGDL NCKLEDERRK VEDLQFQIEE EAISKDDLES RTEVDEEKLR
SLEKDLKREK DRADKSEQEF FTLKAMLKDQ ADRLTSTEDM NMSYLDQIEE LTHKLSQAES
KVKNFESSRL EEGAKRDEIS ANQVKKQKMQ ETINNLTTQL SGRDEASNQL STELQNLKSQ
LAELQRKLES SEEQNNQITE EKMKLEHQMS EMMKNSGDSS NRLSMLNDQV QEKNRKIQDL
QAALSNSTQQ LGRLNDEIEN LKGETIRERE NIISKYEESS KTQSSQIEDL QRELSKAKSK
MQKMTEDHKK DNEDALSRKI KEIEELKKQL QESIEEQERQ AVQTQAHKQV LEKITMEKEA
LQFEKEKTEK QMKRLESEKD SANAELIQAR VEVAKAQSER EKFTADLSAL EEKLQDLGGE
MEKAHKAKSQ IQKELDIIQA EKSKISEEKD HLQDEAISTK ASLQQKDMHI EELQKEVERM
KGEISTQQEM LAQVSQKESS SEAFQQRWEE SQKALAELQT SYSEIEAERD TMKAQLTFAN
LVAEERTRLE DQNQKLNREV EDMQTRHSQE LDELQNANTS LQSQLDNTSQ LLEQKADELD
KQKKQISNLQ NENSSLEVYR SKVQKMETEK KEFLEKISKL ENLLKEAKTN ASNMASNDTA
GNQLTEERDS ALGQVEFLNS VIVDLQKKNS DLKTRLEVME SGVVTNGDGD SSMESEAPKS
RAPPRLFCDI CDVFDKHDTD DCPLQAMDYE DDDAPSPTHY HGDRKASRPY CDICEEFHDP
CPVPDSQEEC QTERADDSPP RLISRSAEQS PKNLQNRDET GVLADATRTQ GLPANHRFLK
NEECNAGSDT PLGDEEVRDG GRELVPGGPK EGKMNDSCRV S
//
