PRTG_MOUSE
ID PRTG_MOUSE Reviewed; 1191 AA.
AC Q2EY15; A4FUS8; A4FUS9; Q2VWP8; Q8BJK6; Q8BYL5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Protogenin;
DE AltName: Full=Protein Shen-Dan;
DE Flags: Precursor;
GN Name=Prtg {ECO:0000312|MGI:MGI:2444710};
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] {ECO:0000305, ECO:0000312|EMBL:ABC96181.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=SWR/J {ECO:0000312|EMBL:ABC96181.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:16881056};
RX PubMed=16881056; DOI=10.1002/dvdy.20898;
RA Vesque C., Anselme I., Couve E., Charnay P., Schneider-Maunoury S.;
RT "Cloning of vertebrate protogenin (Prtg) and comparative expression
RT analysis during axis elongation.";
RL Dev. Dyn. 235:2836-2844(2006).
RN [2] {ECO:0000312|EMBL:AAU05740.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wong Y.-H., Chang C., Chen P.-H., Yu J.-Y., Wang Y.-C., Lee C.-M.,
RA Lin W.-J., Tsai T.-F., Wang A.-G., Fann M.-J.;
RT "Shen-Dan is a novel receptor for embryonic stem cells and developing
RT neurons.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAC38947.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 128-1191.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC38947.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAC38947.1}, and
RC Hypothalamus {ECO:0000312|EMBL:BAC30243.1};
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAI16337.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 129-1191.
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: May play a role in anteroposterior axis elongation.
CC {ECO:0000269|PubMed:16881056}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: From mid-gastrulation to early somite stages,
CC restricted to posterior neural plate and mesoderm with an anterior
CC limit at the level of the rhombencephalon. Posterior restriction is
CC progressively lost during somitogenesis. Expression is maintained in
CC the neural tube and paraxial mesoderm during this process. As
CC development proceeds, further restricted to the dorsal parts of the
CC spinal cord and somites. In parallel, expression progresses caudally
CC during axis elongation. {ECO:0000269|PubMed:16881056}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. DCC family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC38947.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ360114; ABC96181.1; -; mRNA.
DR EMBL; AY630257; AAU05740.1; -; mRNA.
DR EMBL; AK039115; BAC30243.1; -; mRNA.
DR EMBL; AK083540; BAC38947.1; ALT_INIT; mRNA.
DR EMBL; BC116336; AAI16337.1; -; mRNA.
DR EMBL; BC116337; AAI16338.1; -; mRNA.
DR CCDS; CCDS23331.1; -.
DR RefSeq; NP_780694.3; NM_175485.4.
DR AlphaFoldDB; Q2EY15; -.
DR SMR; Q2EY15; -.
DR STRING; 10090.ENSMUSP00000055815; -.
DR GlyGen; Q2EY15; 2 sites.
DR iPTMnet; Q2EY15; -.
DR PhosphoSitePlus; Q2EY15; -.
DR CPTAC; non-CPTAC-3740; -.
DR PaxDb; Q2EY15; -.
DR PeptideAtlas; Q2EY15; -.
DR PRIDE; Q2EY15; -.
DR ProteomicsDB; 291825; -.
DR Antibodypedia; 52034; 73 antibodies from 13 providers.
DR DNASU; 235472; -.
DR Ensembl; ENSMUST00000055535; ENSMUSP00000055815; ENSMUSG00000036030.
DR GeneID; 235472; -.
DR KEGG; mmu:235472; -.
DR UCSC; uc009qqh.1; mouse.
DR CTD; 283659; -.
DR MGI; MGI:2444710; Prtg.
DR VEuPathDB; HostDB:ENSMUSG00000036030; -.
DR eggNOG; KOG4221; Eukaryota.
DR GeneTree; ENSGT00940000155943; -.
DR HOGENOM; CLU_006906_1_0_1; -.
DR InParanoid; Q2EY15; -.
DR OMA; PMNCTTI; -.
DR OrthoDB; 1010015at2759; -.
DR PhylomeDB; Q2EY15; -.
DR TreeFam; TF321506; -.
DR BioGRID-ORCS; 235472; 6 hits in 75 CRISPR screens.
DR ChiTaRS; Prtg; mouse.
DR PRO; PR:Q2EY15; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q2EY15; protein.
DR Bgee; ENSMUSG00000036030; Expressed in primitive streak and 122 other tissues.
DR Genevisible; Q2EY15; MM.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IPI:MGI.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IMP:MGI.
DR CDD; cd00063; FN3; 5.
DR Gene3D; 2.60.40.10; -; 9.
DR InterPro; IPR043204; Basigin-like.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR033011; Protogenin.
DR PANTHER; PTHR10075; PTHR10075; 1.
DR PANTHER; PTHR10075:SF75; PTHR10075:SF75; 1.
DR Pfam; PF00041; fn3; 5.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00060; FN3; 5.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 5.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 2: Evidence at transcript level;
KW Developmental protein; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1191
FT /note="Protogenin"
FT /evidence="ECO:0000255"
FT /id="PRO_5000141192"
FT TOPO_DOM 24..943
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 944..964
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 965..1191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..124
FT /note="Ig-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 126..216
FT /note="Ig-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 229..316
FT /note="Ig-like 3"
FT /evidence="ECO:0000255"
FT DOMAIN 321..405
FT /note="Ig-like 4"
FT /evidence="ECO:0000255"
FT DOMAIN 415..509
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 511..607
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 612..711
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 718..811
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 816..911
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 975..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 150..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 250..298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 342..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 104
FT /note="F -> Y (in Ref. 2; AAU05740)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="Y -> N (in Ref. 2; AAU05740)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="T -> N (in Ref. 3; BAC38947)"
FT /evidence="ECO:0000305"
FT CONFLICT 768
FT /note="Q -> K (in Ref. 3; BAC30243)"
FT /evidence="ECO:0000305"
FT CONFLICT 1185
FT /note="A -> P (in Ref. 4; AAI16338)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1191 AA; 130533 MW; 383250AE82D6171F CRC64;
MAPPVRPGML PLLLLLLLPP LGSVPGVWSF SELFFMKEPQ DATVTRKDPV VLDCQAHGEG
PIKVTWLKNG AKLSENKRIQ VLSNGSLYIS EVEGRRGEQS DEGFYQCLAV NKYGAILSQK
AHLTLSTISA FEVHPVSTEV HEGGVARFSC KISSTPPAVI TWEFNRTALP TTMDRVTALP
SGVLQIYDVG PEDAGNYRCV AATIAHKRKS MEASLTIVAA NETRSFYMPT IIASPQNVTA
SLHQTVVLEC MATGYPRPII SWSRLDHKSI DVFNTRVLGN GNLIISDVKL QHAGVYVCRA
TTPGTRNFTV AMATLTVLAP PSFVEWPESL TRPRAGTARF VCQAEGIPSP KMSWLKNGRR
IHSNGRIKMY NSKLVINQII PEDDAIYQCM AENSQGSVLS RARLTVVMSE DRPSAPYNVH
AETMSSSAIL LAWERPLYNS DKVIAYSVHY MKAEGLNNEE YQVVLGNDTT HYIIDDLEPD
SNYTFYIVAY MPLGASQMSD HVTQNTLEDV PLRPPEISLT SRSPTDILVS WLPIPAKYRR
GQVVLYRLSF RLSTENAIQV VELPGTVHEY LLEGLKPDSV YLVRITAATR VGLGESSVWT
SHRTPKATSV KAPKSPELHL EPLNCTTISV RWLQDTEDPA AIRGYKLFYK EEGQQEHGPI
FLDTGDLLYT LSGLDPRRKY HVRLLAYNNM EEGYQADQTV STPGCVSVRD RMVPPPPPPH
HLYAKANTSS SIFLHWRRPA FTTAQVINYT IRCNPVGLQN ASLVLYLQTS ETHMLVQGLE
PNTKYEFAVR LHVDQLSSPW SPVVYHSTLP EAPTGPPVGV KVTLIEDDTA LVSWKPPDGP
ETVVTRYTIL YASRKAWIAG EWQVLHREGA ITMALLENLV AGNVYIVKIS ASNEVGEGPF
SNSVELAVLP KDASESNQRP KRLDSSNAKV YSGYYHLDQK SMTGIAVGVG IALTCILICV
LILIYRSKAR KSSASKTAQS GTQPLSQASA SVAAGSDMGK NLERATETAE SLVPMMPSSF
IDAKGGTDLI INSYGPIIKN NTKKKWLFFQ DTKKIKVEQT QRRFTQAVCF YQPGTTVLIS
DEDSPGSPGQ TASFPRPFGA TALDTEHSAN SEGSHETGDS GRFSHESNDE IHLSSVISST
PPTSNPLAGG DSDGDAAPKK HGDPAQPLPA EQTSAPQTSA GLRYAAEGFP V
