CKAP4_MOUSE
ID CKAP4_MOUSE Reviewed; 575 AA.
AC Q8BMK4; B2RRB4; Q8BTK8; Q8R3F2;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Cytoskeleton-associated protein 4;
DE AltName: Full=63-kDa cytoskeleton-linking membrane protein;
DE Short=Climp-63;
DE Short=p63;
GN Name=Ckap4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-575.
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Submandibular gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP INTERACTION WITH REEP5, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=32075961; DOI=10.1038/s41467-019-14143-9;
RA Lee S.H., Hadipour-Lakmehsari S., Murthy H.R., Gibb N., Miyake T.,
RA Teng A.C.T., Cosme J., Yu J.C., Moon M., Lim S., Wong V., Liu P.,
RA Billia F., Fernandez-Gonzalez R., Stagljar I., Sharma P., Kislinger T.,
RA Scott I.C., Gramolini A.O.;
RT "REEP5 depletion causes sarco-endoplasmic reticulum vacuolization and
RT cardiac functional defects.";
RL Nat. Commun. 11:965-965(2020).
CC -!- FUNCTION: High-affinity epithelial cell surface receptor for APF.
CC {ECO:0000250}.
CC -!- FUNCTION: Mediates the anchoring of the endoplasmic reticulum to
CC microtubules. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with REEP5. {ECO:0000269|PubMed:32075961}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:32075961}; Single-pass type II membrane protein
CC {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:Q07065}; Single-
CC pass type II membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton.
CC Cytoplasm, perinuclear region. Note=Translocates to the perinuclear
CC region upon APF-stimulation. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in cardiomyocytes (at protein level).
CC {ECO:0000269|PubMed:32075961}.
CC -!- PTM: Reversibly palmitoylated. Palmitoylation at Cys-79 by DHHC2 is
CC required for its trafficking from the ER to the plasma membrane and for
CC its perinuclear localization (By similarity). {ECO:0000250}.
CC -!- PTM: Increased phosphorylation during mitosis prevents binding to
CC microtubules. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25522.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH25522.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Vector contamination at the N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC41005.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC140333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC150314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025522; AAH25522.1; ALT_INIT; mRNA.
DR EMBL; BC138318; AAI38319.1; -; mRNA.
DR EMBL; BC138320; AAI38321.1; -; mRNA.
DR EMBL; AK030708; BAC27092.1; -; mRNA.
DR EMBL; AK089935; BAC41005.1; ALT_INIT; mRNA.
DR CCDS; CCDS24080.1; -.
DR RefSeq; NP_780660.1; NM_175451.1.
DR AlphaFoldDB; Q8BMK4; -.
DR SMR; Q8BMK4; -.
DR BioGRID; 229721; 9.
DR IntAct; Q8BMK4; 4.
DR MINT; Q8BMK4; -.
DR STRING; 10090.ENSMUSP00000050336; -.
DR iPTMnet; Q8BMK4; -.
DR PhosphoSitePlus; Q8BMK4; -.
DR SwissPalm; Q8BMK4; -.
DR EPD; Q8BMK4; -.
DR jPOST; Q8BMK4; -.
DR MaxQB; Q8BMK4; -.
DR PaxDb; Q8BMK4; -.
DR PeptideAtlas; Q8BMK4; -.
DR PRIDE; Q8BMK4; -.
DR ProteomicsDB; 279091; -.
DR Antibodypedia; 613; 303 antibodies from 34 providers.
DR DNASU; 216197; -.
DR Ensembl; ENSMUST00000053871; ENSMUSP00000050336; ENSMUSG00000046841.
DR Ensembl; ENSMUST00000167671; ENSMUSP00000130304; ENSMUSG00000046841.
DR GeneID; 216197; -.
DR KEGG; mmu:216197; -.
DR UCSC; uc007gkq.1; mouse.
DR CTD; 10970; -.
DR MGI; MGI:2444926; Ckap4.
DR VEuPathDB; HostDB:ENSMUSG00000046841; -.
DR eggNOG; ENOG502QVCP; Eukaryota.
DR GeneTree; ENSGT00390000015968; -.
DR HOGENOM; CLU_032481_0_0_1; -.
DR InParanoid; Q8BMK4; -.
DR OMA; EAADTEH; -.
DR OrthoDB; 1255457at2759; -.
DR PhylomeDB; Q8BMK4; -.
DR TreeFam; TF332395; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-5683826; Surfactant metabolism.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR BioGRID-ORCS; 216197; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Ckap4; mouse.
DR PRO; PR:Q8BMK4; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BMK4; protein.
DR Bgee; ENSMUSG00000046841; Expressed in ascending aorta and 235 other tissues.
DR Genevisible; Q8BMK4; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR InterPro; IPR028428; Ckap4.
DR PANTHER; PTHR45161; PTHR45161; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Endoplasmic reticulum; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..575
FT /note="Cytoskeleton-associated protein 4"
FT /id="PRO_0000252418"
FT TOPO_DOM 1..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..575
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 125..193
FT /evidence="ECO:0000255"
FT COILED 236..438
FT /evidence="ECO:0000255"
FT COILED 507..575
FT /evidence="ECO:0000255"
FT COMPBIAS 38..53
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07065"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07065"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07065"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07065"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07065"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 79
FT /note="S-palmitoyl cysteine; by ZDHHC2"
FT /evidence="ECO:0000250"
FT CONFLICT 243
FT /note="K -> M (in Ref. 2; AAH25522)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="M -> I (in Ref. 3; BAC41005)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 575 AA; 63692 MW; 6967F47741C7033D CRC64;
MPSAKQRGSK GGHGAASPSD KGAHPSGGAD DVAKKPPAAP QQPQPPAPHP PQHPQNQAHR
GGHRGRSSAA TANASSASCS RRLGRVLNFL FYLSLVAAAA FSGWYVHHVL EEVQQVRRGH
QDFSRQRDEL GQGLQGVEQK VQSLQATFGT FESLLRNSQH KQDLTEKAVK EGESELNRIS
EVLQKLQNEI LKDLSDGIHV VKDARERDFT SLENTVEERL TELTKSINDN IAIFTDVQKR
SQKEINEVKM KVASLEESKG DRSQDVKTLK DAVKEVQASM MSRERDIEAL KSSLQTMESD
VYTEVRELVS LKQEQQAFKQ AADSERLALQ ALTEKLLRSE ESSSRLPEDI RRLEEELQQL
KVGAHGSEEG AVFKDSKALE ELQRQIEGLG ARLQYVEDGV YSMQVASARH TESLESLLSK
SQEYEQRLAM LQEHVGNLGS SSDLASTVRS LGETQLALSS DLKELKQSLG ELPGTVESLQ
EQVLSLLSQD QAQAEGLPPQ DFLDRLSSLD NLKSSVSQVE SDLKMLRTAV DSLVAYSVKI
ETNENNLESA KGLLDDLRND LDRLFLKVEK IHEKI
