ID A0A1L8GMU3_XENLA Unreviewed; 2630 AA.
AC A0A1L8GMU3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Centrosome-associated protein 350 isoform X3 {ECO:0000313|RefSeq:XP_018114006.1};
GN Name=cep350.L {ECO:0000313|RefSeq:XP_018114006.1,
GN ECO:0000313|Xenbase:XB-GENE-17341571};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018114006.1};
RN [1] {ECO:0000313|RefSeq:XP_018114006.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018114006.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018114006.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_018114006.1; XM_018258517.2.
DR STRING; 8355.A0A1L8GMU3; -.
DR PaxDb; 8355-A0A1L8GMU3; -.
DR GeneID; 108714362; -.
DR KEGG; xla:108714362; -.
DR AGR; Xenbase:XB-GENE-17341571; -.
DR CTD; 108714362; -.
DR Xenbase; XB-GENE-17341571; cep350.L.
DR OMA; ESKHIYC; -.
DR OrthoDB; 2914816at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 108714362; Expressed in muscle tissue and 19 other cell types or tissues.
DR GO; GO:0005813; C:centrosome; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0034453; P:microtubule anchoring; IEA:InterPro.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR028750; CEP350/CC187.
DR PANTHER; PTHR13958:SF3; CAP-GLY DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR13958; CENTROSOME-ASSOCIATED PROTEIN 350; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698}.
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1328..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1588..1632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1707..1734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1774..1829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1935..2000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2052..2103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1231..1283
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1657..1684
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1832..1871
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1597..1632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1716..1734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1774..1823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1935..1979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2076..2091
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2630 AA; 294615 MW; CAF1327E9B9F0876 CRC64;
MDTKKAPSSA TRKISRKDGR YLEDSNTHIS KSVHRSRSSR EKSSRSPLRA TTLESNVKSH
VAFREPLASY RDASASSTPN ERDILQPALG LNAGEREERD FESTRSSAVA NTNVRYLNDP
PAIDALELRL SGSPNELANS ALHTYRGVRA FETLQPNTSF NSSNNRLETL KRRQPDAKLE
KLKERIRRQW ELAGEKDVRE GLHSSAHYSD PTANAKTRKV TSAPPAPVYK GFNPPDKKIS
TLDSKLCKGE DSSQLYGTLQ PSFREGISTN ETSQMKKSSR PVRKVQRLVD GGSTGIPESK
PVKGSIISTS SWRDGQKLVK QLLGPTPKIE KELKGLSDDK HTLKATPPFD GPINKRQGFC
EKDAGKRSVS SERQIKEITK PRGKQIRKRS LSQEKQMENE ELSSKSAASS VGYSEAVREI
DKYCRDPAPT TSSQNDDKIR SHATLDNYNK YQTEPAELKK DFLPLEIQCI LDDLQLDSGI
EGQKQTRGRS KSPTKRKPGK SHAPQEPHIS SKRRHYDTEQ VRLYILRQQE ERKRKHNEEK
EAQKQAEEQK NKRLQELYQK QKEAFSKAKG CATGQYVQER ELQDVIYNHK IEPKIQQPPE
TVPRLMLRHA WSDLSAQEKQ PKVLYQPSGE SDKENKGQER PTSASSGSDL SLSEPLQPLL
RSDLADTYNP TLDNISSKGP LPQSLNQTKG GDLILSRFLT VPKDLESLLS SRKSTANPET
NKTYFQTKPP SNFRTNLDRI ESLKATAVSL SSRIESEAKK LAGGSLAFPS TWGPEPDHIN
NNTTIWKKPD SPPERDGGDD IFSARIQKMI GTCESHFSQK DLPGANDLYK KLPDEFLSNR
NITHGGREVI NDRRPSPGRD ERCRRPTDVS SNTSPLQNSS TSSISEGSLL SEGSLSEGEG
IPRCGSPLFS NKLLKTKAFC MKDQGSKSKS LELLDEFKRE AEKYEPLVTS SAKGPWEELA
KGSPNSVINI FTKSCQLYSK ELDGRLERNS PALKPPYTSA SPQNSVSYAD DFNSCQVSQS
GNQIVRQQSL DTSVSSVNEE LPKSRNEGSS SSSSGARSAS SSASYLSQEG SKLKKSFQND
SSHFPLEDQS SSSSKHKNLA SKHTPLSPGR EPSAGNGTDT DSTIGDLSSR SVTSFDSGRD
VKNRHTNVTE IGAQIPAPTT TTTTGGSVTQ PSDLVSGTVQ GSKHYSPMVL QQRMSAELNY
LSAMEESVRQ LCDVERVRGI SLAQQETVSL AQILKAQQQR HEQNMAALRQ QAEQEAQASL
RQLEDARQKA AQAQAEILQR FQKTLDTSNP LKQDQVLEEL AHSYLSSSSD RTINSLDDPQ
NLQRPFGIWK KESNSLSTSP QPTSSASSIK EHLQSSSCHE SPPTSSVTEA IRSESNTGES
IAEELATPGN ESLQENSIST IHEKDSQSTV SVNEEGMEEQ SFRSLLPSEA HRRGSLERQR
SQRHESDEES TPEKELSGPF ASGQDSFWKF TLEMVRQYMQ EGEMRSAHQS ALLRLRQKAL
KDKTKAELAW LEHLKRRLRD KGEDDKMPPL RKRQRGLLLR LQQEQAEIKR LQEANKAARR
ERQLILKQQE EIQRIQNSTL RLQEKLKSAE NVEHPSELEI QPSSASSHVA SDADSRSPSP
VSVSGSETSS IMQKLRKMHS HMDAKFLTKR EQQLVQRRLH AQELLEWKQR LDEEELEIRH
IEKQALAAWD NQKTNKRSIL DARDKVVEEK NEKEGSSVPS SPSVQTNTSG SLPPEYVASE
LSEAAISEKI LEQTEEHSSI SEELLPLSHS KGSLLQSNKS LRGGESSKDS VVGQQTHTPL
RPHHSSHTWS EESLSITHSE TTSDQSDIEG RIRALKDQLK KRKSVVDSLK REQKKRQKER
LRAQEAILLQ QLKSYDEYIL KTQAELSEEH GTASAPKNAL ASTGTNLTKS DLTSRFVDTP
TYKTVSVNEK QVDFTTDGSV SQEISSASNN EVSKKTTLEH SSVTVSSKDN ESSTIQPRPL
SPPLRDRSLT ATPDSPASSI HSEIPEEMLE SHLSESPLPA ALNLNLRSPT PEEKVYLSRD
HSYSDDFEAS APFRHSVSET PREELEVSYA TTPGRELPSD HEEEHSESRS ASPHVVESST
INPPSHDLLI SSEITDPLAQ LCLGDRVLVS GVQPGTLRFK GTTLFAEGLW AGIELDMPEG
NNDGSHGGSR YFNCKHQYGI FAPPHKITFL SQGKQIQLHK EEYFLSGEAS LDHKNETDVG
LAEPKSEQNA TLEVTEHLIE SQDKTDQNLF LSGDFNLDIT TETPSVKEEE KEPNTPLVDL
LIKDENEPDA LKEQAPNLNI LSESLMQYCL KDTISYIQNL RKQREEKIQQ SNQELHNSPT
TSSLYLNNKE APNDDIHPQL DLAEIEPGCS LLSVFAEEPD WFDEDFGLST CRAQQREMKQ
AQLVEPTPEP CLLVPEPIPK PLLPLLQPEP FLAVPHTALK VEQLVCVAAD ELWKWKELSG
DLQEIRKMYA QDGDEEQNPA RCAYKAVVFD LTHQIFEEIC CSDQMEMQPA WKKPSRVSPT
YARRVRDPHN LEEIKFILID EVLSLLSLKK EQNHKTDWQR MMKFGKKKRD RVDQILVKEL
HEEEAQWVNY DEDELFVKMQ LADGIFEALI QDTVHVLQSI QQKKNLLMLV
//
