PCDBE_MOUSE
ID PCDBE_MOUSE Reviewed; 796 AA.
AC Q6PB90; Q8CCT0; Q91Y05;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Protocadherin beta-14;
DE Short=PCDH-beta-14;
DE Flags: Precursor;
GN Name=Pcdhb14;
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].
RC TISSUE=Brain;
RX PubMed=11230163; DOI=10.1101/gr.167301;
RA Wu Q., Zhang T., Cheng J.-F., Kim Y., Grimwood J., Schmutz J., Dickson M.,
RA Noonan J.P., Zhang M.Q., Myers R.M., Maniatis T.;
RT "Comparative DNA sequence analysis of mouse and human protocadherin gene
RT clusters.";
RL Genome Res. 11:389-404(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 STRUCTURE BY NMR OF 26-137, AND DISULFIDE BOND.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of mouse protocadherin beta 14.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Potential calcium-dependent cell-adhesion protein. May be
CC involved in the establishment and maintenance of specific neuronal
CC connections in the brain.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {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; AY013775; AAK26064.1; -; mRNA.
DR EMBL; AK032156; BAC27730.1; -; mRNA.
DR EMBL; BC059821; AAH59821.1; -; mRNA.
DR CCDS; CCDS29180.1; -.
DR RefSeq; NP_444369.3; NM_053139.3.
DR PDB; 1WYJ; NMR; -; A=26-137.
DR PDBsum; 1WYJ; -.
DR AlphaFoldDB; Q6PB90; -.
DR SMR; Q6PB90; -.
DR STRING; 10090.ENSMUSP00000054111; -.
DR GlyGen; Q6PB90; 4 sites.
DR iPTMnet; Q6PB90; -.
DR PhosphoSitePlus; Q6PB90; -.
DR PaxDb; Q6PB90; -.
DR PRIDE; Q6PB90; -.
DR ProteomicsDB; 289324; -.
DR DNASU; 93885; -.
DR Ensembl; ENSMUST00000052387; ENSMUSP00000054111; ENSMUSG00000044043.
DR GeneID; 93885; -.
DR KEGG; mmu:93885; -.
DR UCSC; uc008epz.1; mouse.
DR CTD; 56122; -.
DR MGI; MGI:2136749; Pcdhb14.
DR VEuPathDB; HostDB:ENSMUSG00000044043; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000163786; -.
DR HOGENOM; CLU_006480_3_0_1; -.
DR InParanoid; Q6PB90; -.
DR OMA; GDIDPCI; -.
DR OrthoDB; 300321at2759; -.
DR PhylomeDB; Q6PB90; -.
DR TreeFam; TF332299; -.
DR BioGRID-ORCS; 93885; 4 hits in 70 CRISPR screens.
DR EvolutionaryTrace; Q6PB90; -.
DR PRO; PR:Q6PB90; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q6PB90; protein.
DR Bgee; ENSMUSG00000044043; Expressed in soleus muscle and 56 other tissues.
DR Genevisible; Q6PB90; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR032455; Cadherin_C.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF16492; Cadherin_C_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell membrane; Disulfide bond;
KW Glycoprotein; Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..796
FT /note="Protocadherin beta-14"
FT /id="PRO_0000271745"
FT TOPO_DOM 30..690
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 691..711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 712..796
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..133
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 138..242
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 247..347
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 352..451
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 456..561
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 568..671
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..102
FT /evidence="ECO:0000269|Ref.4"
FT CONFLICT 122
FT /note="Q -> K (in Ref. 2; BAC27730)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="S -> A (in Ref. 3; AAH59821)"
FT /evidence="ECO:0000305"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1WYJ"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:1WYJ"
FT TURN 49..53
FT /evidence="ECO:0007829|PDB:1WYJ"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:1WYJ"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1WYJ"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1WYJ"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1WYJ"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:1WYJ"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:1WYJ"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:1WYJ"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:1WYJ"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1WYJ"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1WYJ"
SQ SEQUENCE 796 AA; 87022 MW; E5457BFED7E7254B CRC64;
METSLHKAPQ KRQVTAIIFL LLLWEAGSAT ITYSVLEETD RGSLVGNLAK DLGLSLRELI
TRGAQILSKG NKQLLQLEQK SGNLLLKEKL DREELCGSTN PCILHFQVLL KSPVQFIQGE
IQLQDVNDHA PEFMEDEILL KILESSLPGA VFPLKIAQDL DVGSNTVQNY TISTNAHFHL
LTRNHSDGRK YPELVLDKAL DREEQAQIRL TLTAMDSGSP PKTGTTQVVI VVLDINDNAP
EFAQGLYEVQ VQENSPVGSL VLTVSARDLD AGTHGELSYS LFQSSNQVLQ AFEVNTDTGE
IRVRKLLDFE EIQSYRMEIE ASDGGGLSGK CTVVIHVMDV NDNAPELTMS VLISEIPENS
PETIVAIFGI SDPDSGDNGK MVCSVQDRLP FLLKPNEENF YTLVTERALD RESRAEYNIT
ITVSDMGTPR LTTQHTITVQ VSDINDNAPA FTHTSYTMFV RENNSPALHI GTISATDSDS
GSNAHITYSL LPPHDPQLAL NSLISINADN GQLFALRALD YEALQAFEFH VGATDGGSPA
LSSQALVRVV VLDDNDNAPF VLYPMQNASA PCTELLPRAA EPGYLVTKVV AVDRDSGQNA
WLSFQLLKTT EPGLFSVWAH NGEVRTTRLL SERDVPKHRL LLLVKDNGEP PHSASVTLHV
LLVDGFSQPY LPLPEVARDP AQEDVLTLYL VIALASVSSL FLVSVLLFVG VRLCRKAGET
SLGGCSVPEG HFPGHLVDVS GTGTLSQSYQ YEVCLTGGTG TNEFKFLKPV LPNFLNEGGY
RNTEENSNFR DSLGFS
