PCDA9_MOUSE
ID PCDA9_MOUSE Reviewed; 979 AA.
AC Q91Y11;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Protocadherin alpha-9 {ECO:0000312|EMBL:AAK26056.1};
DE Short=PCDH-alpha-9;
DE Flags: Precursor;
GN Name=Pcdha9 {ECO:0000312|EMBL:AAK26056.1};
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 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).
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. {ECO:0000303|PubMed:11230163}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000303|PubMed:11230163};
CC Single-pass type I membrane protein {ECO:0000303|PubMed:11230163}.
CC -!- MISCELLANEOUS: The protocadherins alpha are expressed from a single
CC gene cluster similarly to immunoglobulin and T-cell receptors. The N-
CC terminal region containing the 6 extracellular cadherin domains, unique
CC to each protocadherin alpha, is encoded by one of the large exons found
CC in tandem array within the gene cluster. The C-terminal region,
CC identical to all protocadherins alpha, is encoded by 3 shared exons.
CC {ECO:0000303|PubMed:11230163}.
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; AC020968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY013767; AAK26056.1; -; mRNA.
DR CCDS; CCDS37777.1; -.
DR RefSeq; NP_619602.1; NM_138661.1.
DR AlphaFoldDB; Q91Y11; -.
DR SMR; Q91Y11; -.
DR GlyGen; Q91Y11; 3 sites.
DR iPTMnet; Q91Y11; -.
DR PhosphoSitePlus; Q91Y11; -.
DR PRIDE; Q91Y11; -.
DR ProteomicsDB; 289322; -.
DR Antibodypedia; 45503; 152 antibodies from 20 providers.
DR DNASU; 192161; -.
DR Ensembl; ENSMUST00000115659; ENSMUSP00000111323; ENSMUSG00000103770.
DR GeneID; 192161; -.
DR KEGG; mmu:192161; -.
DR UCSC; uc008epe.2; mouse.
DR CTD; 9752; -.
DR MGI; MGI:2447322; Pcdha9.
DR VEuPathDB; HostDB:ENSMUSG00000103770; -.
DR GeneTree; ENSGT00940000164036; -.
DR HOGENOM; CLU_006480_0_1_1; -.
DR OMA; VIWLNAT; -.
DR OrthoDB; 184745at2759; -.
DR BioGRID-ORCS; 192161; 1 hit in 69 CRISPR screens.
DR PRO; PR:Q91Y11; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q91Y11; protein.
DR Bgee; ENSMUSG00000103770; Expressed in olfactory bulb granule cell layer and 31 other tissues.
DR Genevisible; Q91Y11; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:MGI.
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; IPR031904; Cadherin_CBD.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR Pfam; PF00028; Cadherin; 4.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF15974; Cadherin_tail; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 6.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..59
FT /evidence="ECO:0000255"
FT CHAIN 60..979
FT /note="Protocadherin alpha-9"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431484"
FT TOPO_DOM 60..726
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 727..747
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 748..979
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 64..163
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 164..272
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 273..380
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 381..485
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 486..595
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 611..707
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REPEAT 763..766
FT /note="PXXP 1"
FT REPEAT 828..831
FT /note="PXXP 2"
FT REPEAT 861..864
FT /note="PXXP 3"
FT REPEAT 902..905
FT /note="PXXP 4"
FT REPEAT 920..923
FT /note="PXXP 5"
FT REGION 763..923
FT /note="5 X 4 AA repeats of P-X-X-P"
FT REGION 859..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..979
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 979 AA; 106763 MW; 78098788420924D6 CRC64;
MRLGNRPEDI RTCVHLRWHI HGLLRQENAS VVISKCLRHG AWRLLLWLLL LATWDVGSGQ
LHYSVPEEAK HGTFVGRIAQ DLGLELAELV PRLFRVVSKD RGDLLEVNLQ NGILFVNSRI
DREELCGQNA ECSIHLEVIV DRPLQVFHVE VEVRDINDNP PIFSVAEQKI LVAESRLLDS
RFPLEGASDA DVGENSMLTY KLSSNEFFIL DIVNKRGKGK FPVLVLRKLI DREENPQLKL
LLTATDGGKP EFTGSVSLLI QVLDVNDNAP VFDRSVYEVK MYENQENKTL VIWLNATDSD
EGINKEVEYS FSSLASSIIR QKFLINEKTG EIKINGAIDF EESNNYEIHV DATDKGYPPM
VAHCTVLVEI LDENDNAPEI VLTSLSLPVK EDAPLGSVIA LISVSDKDSG VNGQVTCSLT
NHVPFKLVST FKNYYSLVLD SALDRETTAD YKVVVTARDG GSPSLWATAS VSVEVADVND
NAPAFAHPEY TVFVKENNPP GVHIFTVLAV DADAQENALV SYSLVERRVG ERLLSSYVSV
HAESGKVFAL QPLDHEELEL LQFQVSARDA GVPALGSNVT LQVFVQDEND NPPTLLGHQS
GGPAGEFSQL VSRSVGAGHV VSKVRAVDAD SGYNAWLSYE LHPTVGARSP FRVGLYTGEI
SMTRALDESD LPRQRLLVLV KDHGEPMLIA TATVLVSLVE NGQVPKASSQ GLPNSSRREA
SLMDVNVYLI IAICAVSSLL VLTLLLYTAL RCSAVPMQAG CGLGKPTLVC SSAVGTWSYS
QQRQQRVCSG EGPPKTDLMA FSPSLTPCPV AEVGMESHSV GGDVPGKPRQ PNPDWRYSAS
LRAGMHSSVH LEEAGILRAG PGGPDQQWPT VSSATPEPEA GEVSPPVGAG VNSNSWTFKY
GPGNPKQSGP GELPDKFIIP GSPAIISIRQ EPANNQIDKS DFITFGKKEE TKKKKKKKKG
NKTQEKKEKG NSTTDNSDQ
