PROM2_MOUSE
ID PROM2_MOUSE Reviewed; 835 AA.
AC Q3UUY6; A2AHT1; Q8CDM5; Q8CHT5; Q8R4Y7; Q9WUC7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Prominin-2;
DE Short=PROM-2;
DE AltName: Full=Prominin-like protein 2;
DE Short=mPROML2;
DE Flags: Precursor;
GN Name=Prom2; Synonyms=Proml2;
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=BALB/cJ, and C57BL/6J; 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Skin, and Testis;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [5]
RP GLYCOSYLATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=17874118; DOI=10.1007/s00418-007-0334-2;
RA Jaszai J., Janich P., Farkas L.M., Fargeas C.A., Huttner W.B., Corbeil D.;
RT "Differential expression of prominin-1 (CD133) and prominin-2 in major
RT cephalic exocrine glands of adult mice.";
RL Histochem. Cell Biol. 128:409-419(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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 -!- SUBUNIT: Binds cholesterol. {ECO:0000250}.
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=Colocalizes with PROM1 (By similarity). Associates with membrane
CC in a cholesterol-dependent manner. Localizes to the apical and
CC basolateral membranes of epithelial cells. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UUY6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UUY6-2; Sequence=VSP_033150;
CC -!- TISSUE SPECIFICITY: Expressed in kidney and testis. Present in urine
CC within small membrane particles (at protein level). In the
CC submandibular gland, expressed in seromucous acini. In the parotid
CC gland, expressed in the serous acini and in all segments of the duct
CC system. In the sublingual gland, expressed in large excretory ducts,
CC but absent in intercalated ducts. In the extraorbital lacrimal gland,
CC expressed in the serous acini. In the eyelid, expressed in the acini of
CC the meibomian gland. {ECO:0000269|PubMed:12514187,
CC ECO:0000269|PubMed:17109118, ECO:0000269|PubMed:17874118}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:17109118}.
CC -!- SIMILARITY: Belongs to the prominin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC26644.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF128113; AAD22488.1; -; mRNA.
DR EMBL; AF269062; AAM10543.1; -; mRNA.
DR EMBL; AK029851; BAC26644.1; ALT_FRAME; mRNA.
DR EMBL; AK137749; BAE23487.1; -; mRNA.
DR EMBL; AL731831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039212; AAH39212.1; -; mRNA.
DR CCDS; CCDS16704.1; -. [Q3UUY6-1]
DR CCDS; CCDS50704.1; -. [Q3UUY6-2]
DR RefSeq; NP_620089.2; NM_138750.2. [Q3UUY6-1]
DR RefSeq; NP_835148.2; NM_178047.4. [Q3UUY6-2]
DR AlphaFoldDB; Q3UUY6; -.
DR SMR; Q3UUY6; -.
DR BioGRID; 228680; 1.
DR STRING; 10090.ENSMUSP00000028855; -.
DR GlyGen; Q3UUY6; 1 site.
DR iPTMnet; Q3UUY6; -.
DR PhosphoSitePlus; Q3UUY6; -.
DR MaxQB; Q3UUY6; -.
DR PaxDb; Q3UUY6; -.
DR PeptideAtlas; Q3UUY6; -.
DR PRIDE; Q3UUY6; -.
DR ProteomicsDB; 291529; -. [Q3UUY6-1]
DR ProteomicsDB; 291530; -. [Q3UUY6-2]
DR Antibodypedia; 54175; 327 antibodies from 28 providers.
DR DNASU; 192212; -.
DR Ensembl; ENSMUST00000028855; ENSMUSP00000028855; ENSMUSG00000027376. [Q3UUY6-1]
DR Ensembl; ENSMUST00000103214; ENSMUSP00000099503; ENSMUSG00000027376. [Q3UUY6-2]
DR GeneID; 192212; -.
DR KEGG; mmu:192212; -.
DR UCSC; uc008mfp.2; mouse. [Q3UUY6-1]
DR UCSC; uc012cdo.1; mouse. [Q3UUY6-2]
DR CTD; 150696; -.
DR MGI; MGI:2138997; Prom2.
DR VEuPathDB; HostDB:ENSMUSG00000027376; -.
DR eggNOG; KOG4331; Eukaryota.
DR GeneTree; ENSGT00530000063586; -.
DR HOGENOM; CLU_008293_2_0_1; -.
DR InParanoid; Q3UUY6; -.
DR OMA; VKEQMEP; -.
DR OrthoDB; 1129032at2759; -.
DR PhylomeDB; Q3UUY6; -.
DR TreeFam; TF324631; -.
DR BioGRID-ORCS; 192212; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Prom2; mouse.
DR PRO; PR:Q3UUY6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q3UUY6; protein.
DR Bgee; ENSMUSG00000027376; Expressed in parotid gland and 76 other tissues.
DR Genevisible; Q3UUY6; MM.
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:MGI.
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; ISS:CAFA.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:CAFA.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:CAFA.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0044393; C:microspike; ISS:CAFA.
DR GO; GO:0005902; C:microvillus; ISS:CAFA.
DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0071914; C:prominosome; IDA:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; ISS:CAFA.
DR GO; GO:2001287; P:negative regulation of caveolin-mediated endocytosis; ISO:MGI.
DR GO; GO:0048550; P:negative regulation of pinocytosis; ISO:MGI.
DR GO; GO:0031346; P:positive regulation of cell projection organization; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0043087; P:regulation of GTPase activity; ISO:MGI.
DR InterPro; IPR008795; Prominin.
DR PANTHER; PTHR22730; PTHR22730; 1.
DR Pfam; PF05478; Prominin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cilium; Coiled coil;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..835
FT /note="Prominin-2"
FT /id="PRO_0000331240"
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..435
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..478
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 500..780
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 781..801
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 802..835
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT COILED 646..675
FT /evidence="ECO:0000255"
FT MOD_RES 819
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CJ52"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 815..828
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033150"
FT CONFLICT 660
FT /note="R -> Q (in Ref. 1; AAM10543 and 4; AAH39212)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 835 AA; 93206 MW; FA4EE16CFD3A0D98 CRC64;
MTRSPGLMVP LLGLSLGLAL SLPEAVTDDC GSLGRVEHLA FARVPRTREL APLVRASGPL
NSLYGTVRRF LSVVQLNPFP AELIKTLLND PSSVKTDEVV RYEAGYVVCA VIAGLYLLLV
PITGLCFCCC RCRQRCGGRV KTEHKAMACE RGTLMIFLLL TTLVLLIGMV CAFATNQHTH
SQTGPSVKAV PETLLSLRGL VSDVPEELRA IAEQFSVPQK QVSKELDGVG ENLGNVIHNR
LKSTVYPVLA SVHSLGQALQ VSIDHLRALN TTSVELQEAQ RHLEPPVQAH RERLLALLQD
SWCHEENCKR VLSQAGALQL GADFSQTPPV DDVLHRLKDV PETNFSSMVQ EEKATFNNLP
LLVQVQAVSV VKDVKKALAE QPEGLRMLAQ AFPGSEAASR WSQALEGLEQ RSRPYLQEVQ
QYETYRWILG CVLCSAILLV VICNLLGLSL GIWGLFARED PSHSETKGEA GARLLMAGVA
FSFLFAVPLI LLVFVTFLVG GNVQTLVCRS WESGELYEFA DTPGNLPPSM NLSYLLGLKK
NISIVQAYRQ CKAGAVLWKV LQLNDSYDLD KHLDIKQYTH KIQQELQSFQ VDLKELDLLS
PTARQDLEAL QRSGLEKIHY RGFLVQIQKP VVNTDMWQLA QELEGLAQAQ NDSLLRQQLR
EEARELRSLY QEKVVPQESL VTKLNFSVKT LESLAPSLQV NTSDFLDSVT RLKGELPVQI
NHILRNATEC FLTREMGYFS QYVTWVRAEV TQRIATCQPF STALDNGHVI LCDMMADPWN
AFWFCLGWCT FFLIPSIIFA VKTSKYFRPI RKRLSSTSSE ETQLFHIPRV TSLKL
