PROM2_RAT
ID PROM2_RAT Reviewed; 834 AA.
AC Q8CJ52; Q8R4B6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Prominin-2;
DE Short=PROM-2;
DE AltName: Full=Prominin-like protein 2;
DE Short=rPROML2;
DE AltName: Full=Testosterone-regulated prominin-related protein;
DE Flags: Precursor;
GN Name=Prom2; Synonyms=Proml2, Trprp;
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 [MRNA], INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=12446606; DOI=10.1210/en.2002-220522;
RA Zhang Q., Haleem R., Cai X., Wang Z.;
RT "Identification and characterization of a novel testosterone-regulated
RT prominin-like gene in the rat ventral prostate.";
RL Endocrinology 143:4788-4796(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=12514187; DOI=10.1074/jbc.m210640200;
RA Fargeas C.A., Florek M., Huttner W.B., Corbeil D.;
RT "Characterization of prominin-2, a new member of the prominin family of
RT pentaspan membrane glycoproteins.";
RL J. Biol. Chem. 278:8586-8596(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=12832703; DOI=10.1634/stemcells.21-4-506;
RA Fargeas C.A., Corbeil D., Huttner W.B.;
RT "AC133 antigen, CD133, prominin-1, prominin-2, etc.: prominin family gene
RT products in need of a rational nomenclature.";
RL Stem Cells 21:506-508(2003).
RN [4]
RP INTERACTION WITH CHOLESTEROL, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=17109118; DOI=10.1007/s00441-006-0324-z;
RA Florek M., Bauer N., Janich P., Wilsch-Braeuninger M., Fargeas C.A.,
RA Marzesco A.-M., Ehninger G., Thiele C., Huttner W.B., Corbeil D.;
RT "Prominin-2 is a cholesterol-binding protein associated with apical and
RT basolateral plasmalemmal protrusions in polarized epithelial cells and
RT released into urine.";
RL Cell Tissue Res. 328:31-47(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-818, 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).
CC -!- SUBUNIT: Binds to cholesterol.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane
CC protein. Basolateral cell membrane; Multi-pass membrane protein. Cell
CC projection, microvillus membrane; Multi-pass membrane protein. Cell
CC projection, cilium membrane; Multi-pass membrane protein.
CC Note=Localizes to the apical and basolateral membranes of epithelial
CC cells. Associates with membrane in a cholesterol-dependent manner.
CC Colocalizes with PROM1.
CC -!- TISSUE SPECIFICITY: In the ventral prostate, expressed in glandular
CC epithelial cells. {ECO:0000269|PubMed:12446606}.
CC -!- INDUCTION: Up-regulated by androgen. {ECO:0000269|PubMed:12446606}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:17109118}.
CC -!- SIMILARITY: Belongs to the prominin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM03109.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF486828; AAM03109.1; ALT_FRAME; mRNA.
DR EMBL; AF508942; AAN63818.1; -; mRNA.
DR RefSeq; NP_620212.1; NM_138857.1.
DR AlphaFoldDB; Q8CJ52; -.
DR STRING; 10116.ENSRNOP00000020354; -.
DR GlyGen; Q8CJ52; 1 site.
DR iPTMnet; Q8CJ52; -.
DR PhosphoSitePlus; Q8CJ52; -.
DR jPOST; Q8CJ52; -.
DR PaxDb; Q8CJ52; -.
DR PRIDE; Q8CJ52; -.
DR GeneID; 192211; -.
DR KEGG; rno:192211; -.
DR UCSC; RGD:621435; rat.
DR CTD; 150696; -.
DR RGD; 621435; Prom2.
DR eggNOG; KOG4331; Eukaryota.
DR InParanoid; Q8CJ52; -.
DR OrthoDB; 1129032at2759; -.
DR PhylomeDB; Q8CJ52; -.
DR PRO; PR:Q8CJ52; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0044393; C:microspike; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; TAS:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0071914; C:prominosome; IDA:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; TAS:RGD.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:RGD.
DR GO; GO:2001287; P:negative regulation of caveolin-mediated endocytosis; ISO:RGD.
DR GO; GO:0048550; P:negative regulation of pinocytosis; ISO:RGD.
DR GO; GO:0031346; P:positive regulation of cell projection organization; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0043087; P:regulation of GTPase activity; ISO:RGD.
DR InterPro; IPR008795; Prominin.
DR PANTHER; PTHR22730; PTHR22730; 1.
DR Pfam; PF05478; Prominin; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cilium; Coiled coil; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..834
FT /note="Prominin-2"
FT /id="PRO_0000331241"
FT TOPO_DOM 28..106
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..434
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..779
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 780..800
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 801..834
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT COILED 637..674
FT /evidence="ECO:0000255"
FT MOD_RES 818
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 217
FT /note="S -> L (in Ref. 1; AAM03109)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="L -> I (in Ref. 1; AAM03109)"
FT /evidence="ECO:0000305"
FT CONFLICT 580
FT /note="E -> K (in Ref. 1; AAM03109)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="Q -> H (in Ref. 1; AAM03109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 834 AA; 92841 MW; CE1A53DB5CBEF57A CRC64;
MTRTLDLMVP LLGLSLGLAL SLPRAVAADC GSLGRVEHLA FAPVPGTEPT APRVRAPWPL
DSLYGTVRRF LSVVQLNPFP AELIKTLLND PSSVKTDEVV RYEAGYVVCA VIAGLYLLLV
PITGLCFCCC RCRRRCGGRV KTEHKAMACE RGTLMTFLLL TTLMLLIGMV CAFATNQFTH
SQTGPSVEAV PETLLSLRGL VSDVPKKLQA VADQFSSPQK QVSKDLDGVG ENLGNIIHNQ
LKSTVYPVLA SVHGLGQALQ VSIDHLQSVN ATSVELREGQ QHLGPPVQAH RERLLALLQE
SWCHENCKGA LSQASALQLG ADFSQMPPVD DVLHRLQGVP EANFSSMVQE ENATFNNLPI
LVHMQMVSVV KDLKKALAEQ PEGVRMLAQA FPGSEATSRW SQALEGLEQR SRPYLQDVQR
YETYRWILGC VLCSAILLVV ICNLLGLSLG IWGLFAREDP SHSETKGEAG ARFLMAGVAF
SFLFAAPLIL LVFATFLVGG NVQTLVCRSW ESGELYEFVD TPGNLPPSMN LSYLLGLRKN
ISVFQAYRQC KAGTALWKVL QLNDSYDLDK HLDIKQYTHE LQQELQSFKV DLKDLDLLNP
AARQNLEALQ SSGLEKIHYR DFLVQIQKPV VKTDMGQLAK ELEGLAQAQN ESLRRQQLQE
EARELRSLYQ EKVVPQENLV AKLNPSIRVL ESSAPKLQVN TSDLLDIVAR LKGELPAQLN
HILRNATECF LTREMGYFSQ YVTWVREEVT QHIATCQPFS KALDDGHMIL CDMMANPWNA
FWFCLGWCTF FLIPSIIFAV KTSKYFRPIR KRLSSTSSEE TQLFHIPRVT SLKL
