ID A0A6I8RJT9_XENTR Unreviewed; 2326 AA.
AC A0A6I8RJT9;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 18-JUN-2025, entry version 25.
DE SubName: Full=CAP-Gly domain-containing linker protein 1 {ECO:0000313|Ensembl:ENSXETP00000081059, ECO:0000313|RefSeq:XP_012818415.2};
GN Name=clip1 {ECO:0000313|Ensembl:ENSXETP00000081059,
GN ECO:0000313|RefSeq:XP_012818415.2,
GN ECO:0000313|Xenbase:XB-GENE-1012946};
GN Synonyms=clip-170 {ECO:0000313|RefSeq:XP_012818415.2}, clip170
GN {ECO:0000313|RefSeq:XP_012818415.2};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000081059};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000081059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000081059};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000081059}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-2020) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_012818415.2}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_012818415.2};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_012818415.2};
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR RefSeq; XP_012818415.2; XM_012962961.3.
DR Ensembl; ENSXETT00000068445; ENSXETP00000081059; ENSXETG00000003780.
DR GeneID; 100124823; -.
DR AGR; Xenbase:XB-GENE-1012946; -.
DR Xenbase; XB-GENE-1012946; clip1.
DR Proteomes; UP000008143; Chromosome 1.
DR Bgee; ENSXETG00000003780; Expressed in heart and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR FunFam; 2.30.30.190:FF:000002; CAP-Gly domain containing linker protein 1; 1.
DR FunFam; 2.30.30.190:FF:000001; Putative CAP-Gly domain-containing linker protein 1; 1.
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:SF44; CAP-GLY DOMAIN-CONTAINING LINKER PROTEIN 1; 1.
DR PANTHER; PTHR18916; DYNACTIN 1-RELATED MICROTUBULE-BINDING; 1.
DR Pfam; PF01302; CAP_GLY; 2.
DR Pfam; PF16641; CLIP1_ZNF; 2.
DR SMART; SM01052; CAP_GLY; 2.
DR SUPFAM; SSF74924; Cap-Gly domain; 2.
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:UP000008143};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 75..117
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 230..272
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2103..2127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2175..2199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 349..485
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 517..569
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 603..982
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1012..1206
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1257..1400
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1425..1512
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1573..1705
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 131..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..331
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2112..2123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2183..2196
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2326 AA; 264836 MW; E61FAF4FB4653CD3 CRC64;
MSSLKPSGLK APSRIAKPGT AAAKSSAVTA PTVKTAEKPA STAPSETAEE FVDDFRVGEK
VWVNGNKPGF IQFLGETQFA PGQWAGIVLD EVIGKNDGAV AGVRYFQCEA LRGIFTRPSK
LSRKPLEEES NGTQTAPISR ATSPTSLSCT NVSPVVTTAP TSALTPLKTS TPPAKESSTP
AQLSNLTRTT SESISNLSET GSVKKGEREL KLGDRVLVSG SKAGVIRFLG ETDFAKGEWC
GVELDEPLGK NDGAVAGTRY FQCQPKYGLF APVHKVTRIG FPSTTPAKAK TSVRKIATTP
ATPASLKRSP SASSISSLSS ISSSVSNKPS RTGLLTETSS RYARKISGTT ALQEALKEKQ
QHIEQLLAER DMERAEVAKA TSQVGEVEQE LAVIRHGHDQ YVVEMEAKMD QLRALVEAAD
REKVELLNQL EEEKRKVEDL QFRVEEESIT KGDLEVATVS EKSRIMDLEK DLSLKTKEVV
DLRQRLLQCD KQAGNVDTSL SLLQEVNSLQ ERIATISKEH NHELESLKNK LKNTEENHEK
DLGALKMSTE KISKENETLK VKLNHANKEN SDVIELWKSK LESAITSHQK AMEELTLSFS
KGNSAENSAL IELKAQIENV KIEHQKEMER QKGAQDTDLA GYLKQIEELK AKLQEFNEEK
EMELETMKSK LETAEEQHLI EMEDTLNKLH ESEIKVKELE VLQGKCKEQS ETIDRLTTQM
KSAEDTLVNF DSVQKAESEG KMEIMRYQEN LKAAEVKIKS LEAENSAETS KANDLAKELL
EQKEMLSLSE QKISSFVQIK ESWEKEMEDL KKGLNNSSEN ANLVTKTLQE TVNKLEQKEK
QYEEISKKLD ILKPRCVSLE KMLKESEEKE QNFLSTKTKL EKQISEMIQS SGDSSAQLTK
LNEELQSRER NLDDLRLELS KARDLVHELE EKIALMQSEA ERNNEKAQKS HQEEVEKIAS
QIGDLKLKIE KNQTENKELQ ESHNKIMVDL DVQHQALVTT LKQSIQEKEE LWKTAQATIS
DMKGQMEDLK QEAEQIKSLT CVLESTRNEF ELISEEMRVL KLERDKLAQE TSTLKQGEES
LHLKHLEYES SIKTLQQEQN QLFSMNEELK LENNSLLIKM KELENKNCSL NDGNETLASD
KEKLCYELDN AKQELLKVTM DNEDLQAAVA KMDADLKELQ RSRDLLVTQN EDLQNQKLEL
QDYQKTQTEE KITLAREKDE IIEMLKNTGE EMLNKHKHLT DEISSLQIEK ESAVGKHLEL
ESNLNALISE RDNLLKATTE IKIEREGLML KQNELNTLIE NLHQEKEKLA LERNSKEEEL
IAVTSQLEKL LQENAALLNS KDALTLMCAA VEREKQQLEE CQHQLIDEKM LLAKEKDDII
KALKESQEET STEQKNLVNE LAGLRSENEI ITGKLIQHEN RVSVLVKEQE ELMKTTKELS
SQRDELLLKD KESNLRISDL LQEKEQINHK FSELTAELSS FKKQLVKSTK DNEELKNSKE
TLCNLLEEIK TSRSVTDSER VSLLQEKEEM SASQRKLLAE KDDLLKQIEE ITTISKVSLE
QAILCQNEMK EEINNIKNDK ILISAQLVEL ENKLKSVSEK RSVLRENNNE LLSKEQSLIK
ELIDLKNEYE ILNSSNSSLA QEKKSLTEEL ASLNVRINET AKCVDELTKM KENISESLEQ
TLKEKSDLES EITSILQEKN SLMEDYKKCC LNKEMVLKDK DELQIKFQEL HIGYKGFEQR
LTEERETFAN EKESLLLKNE DLQKILDMVT EEKEQALLMH KEVLTEQHKL VEQKENIENN
MHTLSRENES LQAKNQFHLS NIKELQSNVE SLTKSKLDLQ DSYNSILKTL EDLRCVHEAK
NAELENLVRE KCELILAQEN LMASNRSILK EKETLAKDCE KLSEESVILT KKNDEVSAKT
QQLSNQCQAL LNEKEELLEK CNKLQTLHNT TEAKKDEVCQ MAEESLQIVE KITAEKNKLV
KEKEESVNAM DSLKMLNQKL QNDLKDLSKE HNTVSEENTR NVELVKSECL KTETLRKEME
ELRLLAEQKS QQLAALQEEN LKLAEELGKS KEEVTTNQKL EEERSVLNNQ LLEMKKRESL
RKKEFNEEKA SLQKSLSATS ASITEKDKEL ERLRNEVAEL REKNESARSL QSAVRSLESE
KINLEKRVKN LEKELNDNKR QLNNVSNSSG DSSFSSQFQE EKTSLESQID FLNSVIIDLQ
RKNDELKLKI EKMIEASLNG NNEEEMDNRD SLNGTQSKKK VPPRLFCDIC DCFDLHDTED
CPTQTQLPDS PPHSNFHGSR KEERPYCDIC EVFGHWTNSC NDDETF
//
