PCDG4_MOUSE
ID PCDG4_MOUSE Reviewed; 930 AA.
AC Q91XY4; Q80Y31;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Protocadherin gamma-A4 {ECO:0000312|EMBL:AAK26087.1};
DE Short=PCDH-gamma-A4 {ECO:0000303|PubMed:15964765};
DE Flags: Precursor;
GN Name=Pcdhga4 {ECO:0000312|MGI:MGI:1935216};
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:0000312|EMBL:AAK26087.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAK26087.1};
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] {ECO:0000312|EMBL:AAH49814.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb {ECO:0000312|EMBL:AAH49814.1};
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 [3] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=15964765; DOI=10.1016/j.mcn.2005.05.001;
RA Frank M., Ebert M., Shan W., Phillips G.R., Arndt K., Colman D.R.,
RA Kemler R.;
RT "Differential expression of individual gamma-protocadherins during mouse
RT brain development.";
RL Mol. Cell. Neurosci. 29:603-616(2005).
RN [4] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=19776259; DOI=10.1523/jneurosci.2818-09.2009;
RA Garrett A.M., Weiner J.A.;
RT "Control of CNS synapse development by {gamma}-protocadherin-mediated
RT astrocyte-neuron contact.";
RL J. Neurosci. 29:11723-11731(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 (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y5H4}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O88689};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:O88689}.
CC -!- DEVELOPMENTAL STAGE: Expressed in stage P0-P2 spinal astrocytes, stage
CC P15 hippocampus where expression is detected in some pyramidal neurons,
CC and stage P18 cerebellum where strong expression is detected in a few
CC scattered Purkinje cells and weak expression in neighboring Purkinje
CC cells. {ECO:0000269|PubMed:15964765, ECO:0000269|PubMed:19776259}.
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DR EMBL; AY013798; AAK26087.1; -; mRNA.
DR EMBL; BC049814; AAH49814.1; -; mRNA.
DR CCDS; CCDS79625.1; -.
DR RefSeq; NP_291065.3; NM_033587.3.
DR PDB; 5SZQ; X-ray; 2.61 A; A=237-669.
DR PDBsum; 5SZQ; -.
DR AlphaFoldDB; Q91XY4; -.
DR SMR; Q91XY4; -.
DR GlyGen; Q91XY4; 2 sites.
DR iPTMnet; Q91XY4; -.
DR PhosphoSitePlus; Q91XY4; -.
DR PRIDE; Q91XY4; -.
DR ProteomicsDB; 294343; -.
DR Antibodypedia; 60162; 39 antibodies from 11 providers.
DR DNASU; 93712; -.
DR Ensembl; ENSMUST00000194418; ENSMUSP00000142140; ENSMUSG00000103677.
DR GeneID; 93712; -.
DR KEGG; mmu:93712; -.
DR UCSC; uc008eqp.1; mouse.
DR CTD; 56111; -.
DR MGI; MGI:1935216; Pcdhga4.
DR VEuPathDB; HostDB:ENSMUSG00000103677; -.
DR GeneTree; ENSGT00940000163745; -.
DR HOGENOM; CLU_006480_3_0_1; -.
DR OMA; GLIWICI; -.
DR OrthoDB; 222156at2759; -.
DR BioGRID-ORCS; 93712; 2 hits in 65 CRISPR screens.
DR PRO; PR:Q91XY4; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q91XY4; protein.
DR Bgee; ENSMUSG00000103677; Expressed in cerebellar cortex and 50 other tissues.
DR ExpressionAtlas; Q91XY4; baseline and differential.
DR Genevisible; Q91XY4; 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; IPR032455; Cadherin_C.
DR InterPro; IPR031904; Cadherin_CBD.
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 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 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell membrane; Glycoprotein;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..930
FT /note="Protocadherin gamma-A4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000423520"
FT TOPO_DOM 28..691
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..712
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 713..930
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..132
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 133..241
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 242..346
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 347..451
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 452..561
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 569..682
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 803..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 159
FT /note="L -> P (in Ref. 2; AAH49814)"
FT /evidence="ECO:0000305"
FT STRAND 240..251
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:5SZQ"
FT HELIX 285..290
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:5SZQ"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:5SZQ"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 312..321
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 328..337
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:5SZQ"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 392..397
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:5SZQ"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 415..425
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 432..441
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 450..463
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:5SZQ"
FT HELIX 481..484
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 487..490
FT /evidence="ECO:0007829|PDB:5SZQ"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 508..517
FT /evidence="ECO:0007829|PDB:5SZQ"
FT TURN 521..523
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 526..534
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 536..539
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 543..552
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 560..564
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 573..577
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 586..589
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:5SZQ"
FT HELIX 598..601
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 603..612
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 615..618
FT /evidence="ECO:0007829|PDB:5SZQ"
FT TURN 620..622
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 624..629
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 637..647
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:5SZQ"
FT STRAND 654..663
FT /evidence="ECO:0007829|PDB:5SZQ"
SQ SEQUENCE 930 AA; 100358 MW; 5D52035DB02539BB CRC64;
MAAPYKSDRR GLIWICIFLG SLCDIRAEQI RYSVPEELER GSVVGNLAAD LGLEPGKLAE
RGVRIVSRGK TQLFALNPRS GSLVTAGRVD REGLCDRSPK CTANLEILLE DKVRILAIEV
EIIDVNDNAP SFGAQQREIK VAESENPGTR FPLPEAFDLD IGVNALQGYQ LSSNDHFSLD
VQSGPDGIKY PELVLENALD REEEAVHHLV LTAFDGGDPV RSGTATIQVT LVDTNDNAPV
FTQPEYHISV KENLPVGTRL LTIKATDPDE GVNGEVTYSF RNVREKISQL FQLNSLTGDI
TVLGELDYED SGFYDVDVEA HDGPGLRARS KVLVTVLDVN DNAPEVTVTS LTSSIQEASS
PGTVIALFNV HDSDSGENGL VTCSIPDNLP FRLEKTYGNY HRLLIHRTLD REEVSDYNIT
ITATDQGTPP LSTETYISLQ VVDINDNPPT FTHASYSAYI PENNPRGASI LSITAQDPDS
GENAQVIYSL SEDTIQGAPM SSYVSINSNT GVLYALRSFD YEQFQDLKLL VTARDSGTPP
LSSNVSLSLS VLDQNDNTPE ILYPTIPTDG STGVELTPRS ADPGYLVTKV VAVDKDSGQN
AWLSYRLLKA SEPGLFSVGL HTGEVRTARA LLDRDALKQS LVVTVQDHGQ PPLSATVTLT
IAVSDNIPDI LADLVNINAP IDQEDSDITL YLVVAVAAVS CVFLAFVIVL LIHRLRRWHS
TRLLQAAGNG LSSLPASHFV GVDGVHAFLQ TYSHEVSLTA DSGKSHLIFP QPNYADTLIS
QESCGKSDPL LVSQDLLEIK GDSSLQQAPP NTDWRFSQAQ RPGTSGSQNG DETGTWPNNQ
FDTEMLQAMI LASASEAADG SSTLGGGAGT MGLSARYGPQ FTLQHVPDYR QNVYIPGSNA
TLTNAAGKRD GKAPAGGNGN KKKSGKKEKK
