ID   SDCB2_MOUSE             Reviewed;         292 AA.
AC   Q99JZ0; Q3UN51;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Syntenin-2;
DE   AltName: Full=Syndecan-binding protein 2;
GN   Name=Sdcbp2;
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;
RC   TISSUE=Cecum {ECO:0000312|EMBL:BAE23054.1}, Gall bladder
RC   {ECO:0000312|EMBL:BAE25896.1}, and Stomach
RC   {ECO:0000312|EMBL:BAE35814.1};
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 MRNA].
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).
CC   -!- FUNCTION: Binds phosphatidylinositol 4,5-bisphosphate (PIP2). May play
CC       a role in the organization of nuclear PIP2, cell division and cell
CC       survival. {ECO:0000250|UniProtKB:Q9H190}.
CC   -!- SUBUNIT: Monomer and homodimer. Interacts with SDCBP. Interacts with
CC       TM4SF1. {ECO:0000250|UniProtKB:Q9H190}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H190}.
CC       Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H190}. Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:Q9H190}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q9H190}. Nucleus speckle
CC       {ECO:0000250|UniProtKB:Q9H190}. Note=Associates with intracellular
CC       membranes and enriched in the apical region of the cell and in
CC       intracellular compartments. Colocalizes with TM4SF1 in the apical
CC       region of the cell. Predominantly targeted to nuclear PIP2 pools.
CC       Shuttles between several subcellular compartments. PIP2 plays an
CC       important role in the distribution of SDCBP2.
CC       {ECO:0000250|UniProtKB:Q9H190}.
CC   -!- DOMAIN: The two PDZ domains mediate the interaction with
CC       phosphatidylinositol 4,5-bisphosphate (PIP2) and target SDCBP2 to the
CC       plasma membranes and nucleoli, PIP2-rich regions.
CC       {ECO:0000250|UniProtKB:Q9H190}.
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DR   EMBL; AK136572; BAE23054.1; -; mRNA.
DR   EMBL; AK144452; BAE25896.1; -; mRNA.
DR   EMBL; AK160483; BAE35814.1; -; mRNA.
DR   EMBL; BC005556; AAH05556.1; -; mRNA.
DR   CCDS; CCDS16870.1; -.
DR   RefSeq; NP_663510.1; NM_145535.2.
DR   RefSeq; XP_006499367.1; XM_006499304.2.
DR   RefSeq; XP_006499368.1; XM_006499305.1.
DR   AlphaFoldDB; Q99JZ0; -.
DR   SMR; Q99JZ0; -.
DR   MINT; Q99JZ0; -.
DR   STRING; 10090.ENSMUSP00000028950; -.
DR   PhosphoSitePlus; Q99JZ0; -.
DR   MaxQB; Q99JZ0; -.
DR   PaxDb; 10090-ENSMUSP00000028950; -.
DR   ProteomicsDB; 256758; -.
DR   Antibodypedia; 23059; 256 antibodies from 30 providers.
DR   DNASU; 228765; -.
DR   Ensembl; ENSMUST00000028950.9; ENSMUSP00000028950.9; ENSMUSG00000027456.9.
DR   GeneID; 228765; -.
DR   KEGG; mmu:228765; -.
DR   UCSC; uc008nec.2; mouse.
DR   AGR; MGI:2385156; -.
DR   CTD; 27111; -.
DR   MGI; MGI:2385156; Sdcbp2.
DR   VEuPathDB; HostDB:ENSMUSG00000027456; -.
DR   eggNOG; ENOG502S0HE; Eukaryota.
DR   GeneTree; ENSGT00940000161179; -.
DR   HOGENOM; CLU_059870_0_0_1; -.
DR   InParanoid; Q99JZ0; -.
DR   OMA; AVCEVNG; -.
DR   OrthoDB; 5395964at2759; -.
DR   PhylomeDB; Q99JZ0; -.
DR   TreeFam; TF327131; -.
DR   BioGRID-ORCS; 228765; 3 hits in 77 CRISPR screens.
DR   ChiTaRS; Trappc4; mouse.
DR   PRO; PR:Q99JZ0; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q99JZ0; Protein.
DR   Bgee; ENSMUSG00000027456; Expressed in right colon and 117 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0008283; P:cell population proliferation; ISO:MGI.
DR   CDD; cd00136; PDZ; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   PANTHER; PTHR12345; SYNTENIN RELATED; 1.
DR   PANTHER; PTHR12345:SF13; SYNTENIN-2; 1.
DR   Pfam; PF00595; PDZ; 2.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; PDZ domain-like; 2.
DR   PROSITE; PS50106; PDZ; 2.
DR   Genevisible; Q99JZ0; MM.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasm; Lipid-binding; Membrane; Nucleus;
KW   Reference proteome; Repeat.
FT   CHAIN           1..292
FT                   /note="Syntenin-2"
FT                   /id="PRO_0000184005"
FT   DOMAIN          108..187
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          192..267
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
SQ   SEQUENCE   292 AA;  31565 MW;  C694316BC0A0931D CRC64;
     MSVLYPSLED LKVGQVIQAQ GRASPTMPTL PAPMASAPPL SELYPNLAEL ESYMGLSLSS
     QEVQKNLTQI PDSDNMVVTS PGPGQVVAPV SGNNLGILRA EIKPGVREIH LCKDERGKTG
     LRLQAVDKGL FVQLVQANTP ASLVGLRFGD QILQIDGCDC AGWNTHKAHK VLKKASAEKI
     VMVIRDRPFQ RTVTMHKDSS GQVGFSIKKG KIVSVVKGSS AARNGLLTNH YVCEVNGQNV
     IGLKDKKVTE ILTTAGDVIT LTIIPTVIYE HMIKRLSPLL LHHTMDHSIP DT
//