ID   CYTIP_MOUSE             Reviewed;         359 AA.
AC   Q91VY6; A2AS77; Q3TZH1; Q8R4T4; Q9QZA9;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 142.
DE   RecName: Full=Cytohesin-interacting protein;
DE   AltName: Full=Cytohesin-binding protein HE;
DE            Short=Cbp HE;
DE   AltName: Full=Pleckstrin homology Sec7 and coiled-coil domains-binding protein;
GN   Name=Cytip; Synonyms=Pscdbp;
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 MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Spleen, and Thymus;
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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-36.
RX   PubMed=11850456; DOI=10.1523/jneurosci.22-04-01280.2002;
RA   Kitano J., Kimura K., Yamazaki Y., Soda T., Shigemoto R., Nakajima Y.,
RA   Nakanishi S.;
RT   "Tamalin, a PDZ domain-containing protein, links a protein complex
RT   formation of group 1 metabotropic glutamate receptors and the guanine
RT   nucleotide exchange factor cytohesins.";
RL   J. Neurosci. 22:1280-1289(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-359.
RC   TISSUE=Bone marrow;
RX   PubMed=12909129; DOI=10.1016/s0161-5890(03)00085-3;
RA   Gorski K.S., Shin T., Crafton E., Otsuji M., Rattis F.M., Huang X.,
RA   Kelleher E., Francisco L., Pardoll D., Tsuchiya H.;
RT   "A set of genes selectively expressed in murine dendritic cells: utility of
RT   related cis-acting sequences for lentiviral gene transfer.";
RL   Mol. Immunol. 40:35-47(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, and Spleen;
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).
CC   -!- FUNCTION: By its binding to cytohesin-1 (CYTH1), it modifies activation
CC       of ARFs by CYTH1 and its precise function may be to sequester CYTH1 in
CC       the cytoplasm. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CYTH1 and SNX27. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome
CC       {ECO:0000250}. Note=Recruited from the cytosol to endosomes by SNX27.
CC       {ECO:0000250}.
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DR   EMBL; AK089364; BAC40855.1; -; mRNA.
DR   EMBL; AK152784; BAE31493.1; -; mRNA.
DR   EMBL; AK157859; BAE34237.1; -; mRNA.
DR   EMBL; AK169575; BAE41236.1; -; mRNA.
DR   EMBL; AK170544; BAE41869.1; -; mRNA.
DR   EMBL; AK171467; BAE42473.1; -; mRNA.
DR   EMBL; AK172071; BAE42810.1; -; mRNA.
DR   EMBL; AL928564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC007144; AAH07144.1; -; mRNA.
DR   EMBL; AF374273; AAL87039.1; -; mRNA.
DR   EMBL; AF192525; AAF04842.1; -; mRNA.
DR   CCDS; CCDS16048.1; -.
DR   RefSeq; NP_631939.1; NM_139200.4.
DR   RefSeq; XP_006498075.1; XM_006498012.3.
DR   RefSeq; XP_006498076.1; XM_006498013.3.
DR   AlphaFoldDB; Q91VY6; -.
DR   SMR; Q91VY6; -.
DR   STRING; 10090.ENSMUSP00000028175; -.
DR   iPTMnet; Q91VY6; -.
DR   PhosphoSitePlus; Q91VY6; -.
DR   EPD; Q91VY6; -.
DR   jPOST; Q91VY6; -.
DR   MaxQB; Q91VY6; -.
DR   PaxDb; 10090-ENSMUSP00000028175; -.
DR   ProteomicsDB; 279139; -.
DR   Antibodypedia; 1992; 159 antibodies from 31 providers.
DR   DNASU; 227929; -.
DR   Ensembl; ENSMUST00000028175.7; ENSMUSP00000028175.7; ENSMUSG00000026832.13.
DR   GeneID; 227929; -.
DR   KEGG; mmu:227929; -.
DR   UCSC; uc008jsi.1; mouse.
DR   AGR; MGI:2183535; -.
DR   CTD; 9595; -.
DR   MGI; MGI:2183535; Cytip.
DR   VEuPathDB; HostDB:ENSMUSG00000026832; -.
DR   eggNOG; KOG3528; Eukaryota.
DR   GeneTree; ENSGT00530000063734; -.
DR   HOGENOM; CLU_058640_1_0_1; -.
DR   InParanoid; Q91VY6; -.
DR   OMA; SVRKHIF; -.
DR   OrthoDB; 5356422at2759; -.
DR   PhylomeDB; Q91VY6; -.
DR   TreeFam; TF316315; -.
DR   BioGRID-ORCS; 227929; 3 hits in 75 CRISPR screens.
DR   ChiTaRS; Cytip; mouse.
DR   PRO; PR:Q91VY6; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q91VY6; Protein.
DR   Bgee; ENSMUSG00000026832; Expressed in peripheral lymph node and 112 other cell types or tissues.
DR   GO; GO:0005938; C:cell cortex; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0030155; P:regulation of cell adhesion; ISO:MGI.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   PANTHER; PTHR15963:SF1; CYTOHESIN-INTERACTING PROTEIN; 1.
DR   PANTHER; PTHR15963; GENERAL RECEPTOR FOR PHOSPHOINOSITIDES 1-ASSOCIATED SCAFFOLD PROTEIN-RELATED; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   Genevisible; Q91VY6; MM.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Endosome; Reference proteome.
FT   CHAIN           1..359
FT                   /note="Cytohesin-interacting protein"
FT                   /id="PRO_0000097062"
FT   DOMAIN          77..166
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          166..188
FT                   /note="Interaction with CYTH1"
FT                   /evidence="ECO:0000250"
FT   COILED          165..188
FT                   /evidence="ECO:0000255"
FT   CONFLICT        6
FT                   /note="F -> Q (in Ref. 5; AAF04842)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   359 AA;  40143 MW;  4C922BC8B96B11F7 CRC64;
     MSLQRFLQRQ GSNGNLEYCA DSAYGSYSVL TGQLTMEDNR RIQVLADTVA TLPRGRKQLA
     LARSSSLGDF SWSQRKVVTV EKQDNGTFGF EIQTYRLQNQ NICSSEVCTM ICKVQEDSPA
     HCAGLQVGDI FANVNGVSTE GFTHKQVVDL IRSSGNLLTI ETLNGTMIHR RAELEAKLQT
     LKQTLKKKWV ELRSLHLQEQ RLLHGDTANS PNLENMDLDE SSLFGNLLGP SPALLDRHRL
     SSESSCKSWL SSLTVDSEDG YRSSMSEDSI RGAFSRQTST DDECFHSKDG DEILRNASSR
     RNRSISVTSS GSFSPLWESN YSSVFGTLPR KSRRGSVRKQ ILKFIPGLHR AVEEEESRF
//