CLIP1_CHICK
ID CLIP1_CHICK Reviewed; 1433 AA.
AC O42184; O42228; O57563; O57564;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=CAP-Gly domain-containing linker protein 1;
DE AltName: Full=Cytoplasmic linker protein 170;
DE Short=CLIP-170;
DE AltName: Full=Restin;
GN Name=CLIP1; Synonyms=RSN;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9469933; DOI=10.1016/s0378-1119(97)00585-4;
RA Griparic L., Volosky J.M., Keller T.C. III;
RT "Cloning and expression of chicken CLIP-170 and restin isoforms.";
RL Gene 206:195-208(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-1139 (ISOFORMS 3 AND 4).
RC TISSUE=Pectoralis muscle;
RX PubMed=9784600; DOI=10.1016/s0167-4889(98)00096-2;
RA Griparic L., Keller T.C. III;
RT "Identification and expression of two novel CLIP-170/Restin isoforms
RT expressed predominantly in muscle.";
RL Biochim. Biophys. Acta 1405:35-46(1998).
CC -!- FUNCTION: Binds to the plus end of microtubules and regulates the
CC dynamics of the microtubule cytoskeleton. Promotes microtubule growth
CC and microtubule bundling. Links cytoplasmic vesicles to microtubules
CC and thereby plays an important role in intracellular vesicle
CC trafficking. Plays a role macropinocytosis and endosome trafficking.
CC {ECO:0000250|UniProtKB:P30622}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30622}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P30622}. Cytoplasmic
CC vesicle membrane {ECO:0000250|UniProtKB:P30622}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection,
CC ruffle {ECO:0000250|UniProtKB:P30622}. Note=Localizes to microtubule
CC plus ends. Localizes preferentially to the ends of tyrosinated
CC microtubules. Accumulates in plasma membrane regions with ruffling and
CC protrusions. Associates with the membranes of intermediate
CC macropinocytic vesicles. {ECO:0000250|UniProtKB:P30622}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=O42184-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O42184-2; Sequence=VSP_000761;
CC Name=3; Synonyms=CLIP-170(11);
CC IsoId=O42184-3; Sequence=VSP_000762, VSP_000763;
CC Name=4; Synonyms=CLIP-170(11+35);
CC IsoId=O42184-4; Sequence=VSP_000764;
CC -!- DOMAIN: Intramolecular interaction between the zinc finger domain and
CC the CAP-Gly domains may inhibit interaction with tubulin.
CC {ECO:0000250|UniProtKB:P30622}.
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DR EMBL; AF014012; AAC60344.1; -; mRNA.
DR EMBL; AF020764; AAC60345.1; -; mRNA.
DR EMBL; AF045650; AAC03547.1; -; mRNA.
DR EMBL; AF045651; AAC03548.1; -; mRNA.
DR RefSeq; NP_990273.1; NM_204942.1. [O42184-1]
DR AlphaFoldDB; O42184; -.
DR SMR; O42184; -.
DR STRING; 9031.ENSGALP00000007101; -.
DR PaxDb; O42184; -.
DR Ensembl; ENSGALT00000007113; ENSGALP00000007101; ENSGALG00000004467. [O42184-1]
DR Ensembl; ENSGALT00000052776; ENSGALP00000044930; ENSGALG00000004467. [O42184-2]
DR Ensembl; ENSGALT00000091243; ENSGALP00000067447; ENSGALG00000004467. [O42184-4]
DR Ensembl; ENSGALT00000106281; ENSGALP00000069338; ENSGALG00000004467. [O42184-3]
DR GeneID; 395784; -.
DR KEGG; gga:395784; -.
DR CTD; 6249; -.
DR VEuPathDB; HostDB:geneid_395784; -.
DR eggNOG; KOG4568; Eukaryota.
DR GeneTree; ENSGT00940000155122; -.
DR InParanoid; O42184; -.
DR OMA; HQANEAQ; -.
DR OrthoDB; 1110101at2759; -.
DR PhylomeDB; O42184; -.
DR TreeFam; TF326096; -.
DR PRO; PR:O42184; -.
DR Proteomes; UP000000539; Chromosome 15.
DR Bgee; ENSGALG00000004467; Expressed in muscle tissue and 13 other tissues.
DR ExpressionAtlas; O42184; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IBA:GO_Central.
DR Gene3D; 2.30.30.190; -; 2.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR032108; CLIP1_ZNF.
DR Pfam; PF01302; CAP_GLY; 2.
DR Pfam; PF16641; CLIP1_ZNF; 2.
DR SMART; SM01052; CAP_GLY; 2.
DR SUPFAM; SSF74924; SSF74924; 2.
DR PROSITE; PS00845; CAP_GLY_1; 2.
DR PROSITE; PS50245; CAP_GLY_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Membrane; Metal-binding; Microtubule;
KW Reference proteome; Repeat; Transport; Zinc; Zinc-finger.
FT CHAIN 1..1433
FT /note="CAP-Gly domain-containing linker protein 1"
FT /id="PRO_0000083528"
FT DOMAIN 79..121
FT /note="CAP-Gly 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT DOMAIN 235..277
FT /note="CAP-Gly 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT ZN_FING 1412..1429
FT /note="CCHC-type"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 351..1353
FT /evidence="ECO:0000255"
FT COMPBIAS 133..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 458..492
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000761"
FT VAR_SEQ 458..492
FT /note="TQTKLEHARIKELEQSLLFEKTKADKLQRELEDTR -> RKRQISEDPEN
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9784600"
FT /id="VSP_000762"
FT VAR_SEQ 458
FT /note="T -> RKRQISEDPENT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9784600"
FT /id="VSP_000764"
FT VAR_SEQ 803
FT /note="S -> GGSSKVS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9784600"
FT /id="VSP_000763"
FT CONFLICT 309
FT /note="K -> R (in Ref. 2; AAC03547)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="E -> V (in Ref. 2; AAC03548)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1433 AA; 161027 MW; 5631CE8683498E23 CRC64;
MSMLKPSGLK APSKTIKHGS TLLKAPASVA TAPAEKAPSS EKSSSTTTAD AHDDFVDDFR
VGERVWVNGN KPGFIQFLGE TQFAPGQWAG IVLDEPIGKN DGSVAGVRYF QCEPLRGIFT
RPSKLSRKVL TEDEANGTQT AHASRATSPT STSTASAVSA SPAALLPSGI PQKTSPLAAK
EHSTPSQFSN LSKTASGSVS NLSEAGSLKK GERELKIGDR VLVGGTKAGV VRFLGETDFA
KGEWCGVELD EPLGKNDGAV AGTRYFQCQP RYGLFAPVHK VTKIGFPSTT PAKAKTTVRK
VVATPAALKR SPSASSLSSL SSVASSVSSK PSRTGLLTET SSRYARKISG TTALQEALKE
KQQHIEQLLA ERDLERAEVA KATSHVGEIE QELALVRDGH DRHVLEMEAK MDQLRAMVEA
ADREKVELLN QLEEEKRKVE DLQFRVEEES ITKGDLETQT KLEHARIKEL EQSLLFEKTK
ADKLQRELED TRVATVSEKS RIMELERDLA LRVKEVAELR GRLESSKHID DVDTSLSLLQ
EISSLQEKMA AAGKEHQREM SSLKEKFESS EEALRKEIKT LSASNERMGK ENESLKTKLD
HANKENSDVI ELWKSKLESA IASHQQAMEE LKVSFNKGVG AQTAEFAELK TQMEKVKLDY
ENEMSNLKLK QENEKSQHLK EIEALKAKLL EVTEEKEQTL ENLKAKLESV EDQHLVEMED
TLNKLQEAEI KVKELDVLQA KCNEQTKLIG SLTQQIRASE EKLLDLAALQ KANSEGKLEI
QKLSEQLQAA EKQIQNLETE KVSNLTKELQ GKEQKLLDLE KNLSAVNQVK DSLEKELQLL
KEKFTSAVDG AENAQRAMQE TINKLNQKEE QFALMSSELE QLKSNLTVME TKLKEREERE
QQLTEAKVKL ENDIAEIMKS SGDSSAQLMK MNDELRLKER QLEQIQLELT KANEKAVQLQ
KNVEQTAQKA EQSQQETLKT HQEELKKMQD QLTDMKKQME TSQNQYKDLQ AKYEKETSEM
ITKHDADIKG FKQNLLDAEE ALKAAQKKND ELETQAEELK KQAEQAKADK RAEEVLQTME
KVTKEKDAIH QEKIETLASL ENSRQTNEKL QNELDMLKQN NLKNEEELTK SKELLNLENK
KVEELKKEFE ALKLAAAQKS QQLAALQEEN VKLAEELGRS RDEVTSHQKL EEERSVLNNQ
LLEMKKREST LKKEIDEERA SLQKSISDTS ALITQKDEEL EKLRNEITVL RGENASAKTL
QSVVKTLESD KLKLEEKVKN LEQKLKAKSE QPLTVTSPSG DIAANLLQDE SAEDKQQEID
FLNSVIVDLQ RRNEELNLKI QRMCEAALNG NEEETINYDS EEEGLSKKTP RLFCDICGCF
DLHDTEDCPT QAQMLEEPPH STYHGSRREE RPYCDTCEMF GHWTADCNDD ETF
