ID   SDCB2_RAT               Reviewed;         296 AA.
AC   Q4KLN0;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Syntenin-2;
DE   AltName: Full=Syndecan-binding protein 2;
GN   Name=Sdcbp2;
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 {ECO:0000312|EMBL:AAH99095.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta {ECO:0000312|EMBL:AAH99095.1};
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   INTERACTION WITH SDCBP.
RC   TISSUE=Fetal brain;
RX   PubMed=11152476; DOI=10.1074/jbc.m010647200;
RA   Koroll M., Rathjen F.G., Volkmer H.;
RT   "The neural cell recognition molecule neurofascin interacts with syntenin-1
RT   but not with syntenin-2, both of which reveal self-associating activity.";
RL   J. Biol. Chem. 276:10646-10654(2001).
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 (PubMed:11152476).
CC       Interacts with TM4SF1. {ECO:0000250|UniProtKB:Q9H190,
CC       ECO:0000269|PubMed:11152476}.
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; AABR07054304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07054305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH474050; EDL86113.1; -; Genomic_DNA.
DR   EMBL; BC099095; AAH99095.1; -; mRNA.
DR   RefSeq; NP_001020863.1; NM_001025692.1.
DR   RefSeq; XP_017447262.1; XM_017591773.1.
DR   AlphaFoldDB; Q4KLN0; -.
DR   SMR; Q4KLN0; -.
DR   STRING; 10116.ENSRNOP00000012690; -.
DR   PaxDb; Q4KLN0; -.
DR   Ensembl; ENSRNOT00000012690; ENSRNOP00000012690; ENSRNOG00000009528.
DR   GeneID; 311532; -.
DR   KEGG; rno:311532; -.
DR   UCSC; RGD:1307709; rat.
DR   CTD; 27111; -.
DR   RGD; 1307709; Sdcbp2.
DR   eggNOG; ENOG502S0HE; Eukaryota.
DR   GeneTree; ENSGT00940000161179; -.
DR   HOGENOM; CLU_059870_0_0_1; -.
DR   InParanoid; Q4KLN0; -.
DR   OMA; AVCEVNG; -.
DR   OrthoDB; 1035679at2759; -.
DR   PhylomeDB; Q4KLN0; -.
DR   TreeFam; TF327131; -.
DR   PRO; PR:Q4KLN0; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Proteomes; UP000234681; Chromosome 3.
DR   Bgee; ENSRNOG00000009528; Expressed in duodenum and 14 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0016607; C:nuclear speck; ISO:RGD.
DR   GO; GO:0005730; C:nucleolus; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:RGD.
DR   GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR   Gene3D; 2.30.42.10; -; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   Pfam; PF00595; PDZ; 2.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; SSF50156; 2.
DR   PROSITE; PS50106; PDZ; 2.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Lipid-binding; Membrane; Nucleus;
KW   Reference proteome; Repeat.
FT   CHAIN           1..296
FT                   /note="Syntenin-2"
FT                   /id="PRO_0000441797"
FT   DOMAIN          112..191
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          196..271
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
SQ   SEQUENCE   296 AA;  31965 MW;  7F9D098BEC033C18 CRC64;
     MSVLYPSLED LKVGQVIQAQ ARASPMMPTV MPTLPASMAS APPLSELYPN LAELESYMGL
     SLSSQEVQKN LSQIPDGDNM VITSPGPGQV TAPVSGNDLG VLRAEIKPGV REIHLCKDER
     GKTGLRLQAV DKGLFVQLVQ ANTPASLVGL RFGDQILQID GCDCAGWSTH KAQKALKKAS
     AEKIVMVVRD RPFQRTVTMH KDSSGQVGFF IKKGKIVSVV KGSSAARNGL LTNHYVCEVN
     GQNVIGLKDK KIIEILTTAG NVITLTIIPT VIYEHMIKKL SPLLLHHTMD HSIPDT