ID   CLIP4_RAT               Reviewed;         599 AA.
AC   Q66HD5;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=CAP-Gly domain-containing linker protein 4;
DE   AltName: Full=Restin-like protein 2;
GN   Name=Clip4; Synonyms=Rsnl2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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DR   EMBL; BC081910; AAH81910.1; -; mRNA.
DR   RefSeq; NP_001013964.1; NM_001013942.1.
DR   AlphaFoldDB; Q66HD5; -.
DR   SMR; Q66HD5; -.
DR   STRING; 10116.ENSRNOP00000063078; -.
DR   iPTMnet; Q66HD5; -.
DR   PhosphoSitePlus; Q66HD5; -.
DR   PaxDb; Q66HD5; -.
DR   PRIDE; Q66HD5; -.
DR   GeneID; 298801; -.
DR   KEGG; rno:298801; -.
DR   UCSC; RGD:1311049; rat.
DR   CTD; 79745; -.
DR   RGD; 1311049; Clip4.
DR   eggNOG; KOG4568; Eukaryota.
DR   InParanoid; Q66HD5; -.
DR   OrthoDB; 482616at2759; -.
DR   PRO; PR:Q66HD5; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0035371; C:microtubule plus-end; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR   Gene3D; 1.25.40.20; -; 1.
DR   Gene3D; 2.30.30.190; -; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR036859; CAP-Gly_dom_sf.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR028397; CLIP4.
DR   PANTHER; PTHR18916:SF32; PTHR18916:SF32; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01302; CAP_GLY; 2.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM01052; CAP_GLY; 2.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF74924; SSF74924; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 2.
PE   1: Evidence at protein level;
KW   ANK repeat; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..599
FT                   /note="CAP-Gly domain-containing linker protein 4"
FT                   /id="PRO_0000083531"
FT   REPEAT          65..101
FT                   /note="ANK 1"
FT   REPEAT          149..180
FT                   /note="ANK 2"
FT   REPEAT          186..215
FT                   /note="ANK 3"
FT   DOMAIN          303..345
FT                   /note="CAP-Gly 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT   DOMAIN          505..547
FT                   /note="CAP-Gly 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT   REGION          387..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          565..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..434
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..480
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..593
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         557
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   599 AA;  64645 MW;  82DAD16A014DCE21 CRC64;
     MTIEDLPDIP LEGSSLIGRY PFLFTGSDTS VIFSISAAPM PSDCEFSFFD PNDASCQEIL
     FDPKTSVSEL FAILRQWVPQ VQQNIDIIGN EILKRGCNVN DRDGLTDMTL LHYTCKSGAH
     GIGDVETAVK FAAQLIDLGA DASLRSRWTN MNALHYASYF DVPELIRVLL KTSKPKDVDA
     TCSDFNFGTA LHIAAHNLCA GAVKTLLELG ANPAFRNDKG QIPADVVPDP VDMPLEMADA
     AAIAKEIKQM LLDSMPLPCT ITKATLPNCD ITTSKAMLTT LGLKLGDRVV IAGQKVGTLR
     FCGTTEFASG QWAGIELDEP EGKNNGSVGR VQYFKCAPKY GIFAPLSKIT KVKDGRKNIT
     HTPSTKATLH ARSQKVDVAH VTSKVNSGLM TSKKENASES TLSLPRSEEL KTVAKNDATQ
     PGCISSSSST SSLDHKQSHP KKLSTSSSSG KKTLSKSPSL PSRASAGLKS STTSAANNTH
     REGALRLGER VLVVGQRVGT IKFFGTTNFA PGYWYGIELE KPHGKNDGSV GGVQYFSCSP
     RYGIFAPPSR VQRLSDSLDT LSEISSNKQN HSYPGFRRSF STTSASSQKE INRRNAFAK