PCDGF_HUMAN
ID PCDGF_HUMAN Reviewed; 929 AA.
AC Q9Y5G1; A7E229; Q9Y5C7;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2017, sequence version 4.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Protocadherin gamma-B3;
DE Short=PCDH-gamma-B3;
DE Flags: Precursor;
GN Name=PCDHGB3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT VAL-28.
RC TISSUE=Brain;
RX PubMed=10380929; DOI=10.1016/s0092-8674(00)80789-8;
RA Wu Q., Maniatis T.;
RT "A striking organization of a large family of human neural cadherin-like
RT cell adhesion genes.";
RL Cell 97:779-790(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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: 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:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y5G1-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q9Y5G1-2; Sequence=VSP_008688, VSP_008689;
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DR EMBL; AF152332; AAD43726.1; -; mRNA.
DR EMBL; AF152519; AAD43779.1; -; mRNA.
DR EMBL; AC005366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61951.1; -; Genomic_DNA.
DR EMBL; BC150172; AAI50173.1; -; mRNA.
DR CCDS; CCDS58980.1; -. [Q9Y5G1-1]
DR CCDS; CCDS75334.1; -. [Q9Y5G1-2]
DR RefSeq; NP_061747.2; NM_018924.4. [Q9Y5G1-1]
DR RefSeq; NP_115268.2; NM_032097.2. [Q9Y5G1-2]
DR PDB; 5K8R; X-ray; 2.50 A; A=31-444.
DR PDB; 6MEQ; X-ray; 2.90 A; A=31-444.
DR PDB; 6MER; X-ray; 3.00 A; A=31-444.
DR PDBsum; 5K8R; -.
DR PDBsum; 6MEQ; -.
DR PDBsum; 6MER; -.
DR AlphaFoldDB; Q9Y5G1; -.
DR SMR; Q9Y5G1; -.
DR BioGRID; 121042; 7.
DR IntAct; Q9Y5G1; 3.
DR STRING; 9606.ENSP00000461862; -.
DR GlyGen; Q9Y5G1; 3 sites.
DR iPTMnet; Q9Y5G1; -.
DR PhosphoSitePlus; Q9Y5G1; -.
DR BioMuta; PCDHGB3; -.
DR DMDM; 442570291; -.
DR EPD; Q9Y5G1; -.
DR jPOST; Q9Y5G1; -.
DR MassIVE; Q9Y5G1; -.
DR MaxQB; Q9Y5G1; -.
DR PaxDb; Q9Y5G1; -.
DR PeptideAtlas; Q9Y5G1; -.
DR PRIDE; Q9Y5G1; -.
DR ProteomicsDB; 86363; -. [Q9Y5G1-1]
DR ProteomicsDB; 86364; -. [Q9Y5G1-2]
DR Antibodypedia; 62672; 22 antibodies from 13 providers.
DR DNASU; 56102; -.
DR Ensembl; ENST00000576222.2; ENSP00000461862.1; ENSG00000262209.3. [Q9Y5G1-1]
DR Ensembl; ENST00000618934.1; ENSP00000483339.1; ENSG00000262209.3. [Q9Y5G1-2]
DR GeneID; 56102; -.
DR KEGG; hsa:56102; -.
DR MANE-Select; ENST00000576222.2; ENSP00000461862.1; NM_018924.5; NP_061747.2.
DR UCSC; uc003ljw.3; human. [Q9Y5G1-1]
DR CTD; 56102; -.
DR GeneCards; PCDHGB3; -.
DR HGNC; HGNC:8710; PCDHGB3.
DR HPA; ENSG00000262209; Tissue enhanced (brain).
DR MIM; 604968; gene.
DR MIM; 606301; gene.
DR neXtProt; NX_Q9Y5G1; -.
DR PharmGKB; PA33058; -.
DR VEuPathDB; HostDB:ENSG00000262209; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000163837; -.
DR HOGENOM; CLU_006480_3_0_1; -.
DR InParanoid; Q9Y5G1; -.
DR OMA; HHTTYCK; -.
DR OrthoDB; 305110at2759; -.
DR PhylomeDB; Q9Y5G1; -.
DR TreeFam; TF332299; -.
DR PathwayCommons; Q9Y5G1; -.
DR SignaLink; Q9Y5G1; -.
DR SIGNOR; Q9Y5G1; -.
DR BioGRID-ORCS; 56102; 9 hits in 1019 CRISPR screens.
DR GenomeRNAi; 56102; -.
DR Pharos; Q9Y5G1; Tdark.
DR PRO; PR:Q9Y5G1; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9Y5G1; protein.
DR Bgee; ENSG00000262209; Expressed in stromal cell of endometrium and 96 other tissues.
DR Genevisible; Q9Y5G1; HS.
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 GO; GO:0007399; P:nervous system development; IEA:UniProt.
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; Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Glycoprotein; Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..929
FT /note="Protocadherin gamma-B3"
FT /id="PRO_0000003976"
FT TOPO_DOM 31..691
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..712
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 713..929
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..133
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 134..242
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 243..347
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 348..452
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 453..562
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 570..675
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 791..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 806..814
FT /note="QAPPNTDWR -> VSFFKPFLP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10380929"
FT /id="VSP_008688"
FT VAR_SEQ 815..929
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10380929"
FT /id="VSP_008689"
FT VARIANT 20
FT /note="F -> Y (in dbSNP:rs6860590)"
FT /id="VAR_048569"
FT VARIANT 28
FT /note="A -> V (in dbSNP:rs6860609)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_061073"
FT VARIANT 389
FT /note="N -> K (in dbSNP:rs2240697)"
FT /id="VAR_048570"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:5K8R"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:5K8R"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:5K8R"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:5K8R"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:5K8R"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:5K8R"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:5K8R"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:5K8R"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:6MEQ"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:5K8R"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 206..220
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 223..233
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 245..252
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:5K8R"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:5K8R"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:5K8R"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:5K8R"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 313..322
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 328..338
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 346..352
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 365..372
FT /evidence="ECO:0007829|PDB:5K8R"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 382..388
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 391..396
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 398..406
FT /evidence="ECO:0007829|PDB:5K8R"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 417..426
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:5K8R"
FT STRAND 433..443
FT /evidence="ECO:0007829|PDB:5K8R"
SQ SEQUENCE 929 AA; 101204 MW; 04342DAE4383B295 CRC64;
MGNSSGWRGP AGQRRMLFLF LLSLLDQALS EPIRYAIPEE LDRGSLVGNL AKDLGFGVGD
LPTRNLRVIA EKKFFTVSPE NGNLLVSDRI DREEICGKKS TCVLEFEMVA EKPLNFFHVT
VLIQDINDNP PTFSQNITEL EISELALTGA TFALESAQDP DVGVNSLQQY YLSPDPHFSL
IQKENLDGSR YPELVLKAPL DREEQPHHHL VLTAVDGGEP SRSCTTQIRV IVADANDNPP
VFTQDMYRVN VAENLPAGSS VLKVMAIDMD EGINAEIIYA FINIGKEVRQ LFKLDSKTGE
LTTIGELDFE ERDSYTIGVE AKDGGHHTAY CKVQIDISDE NDNAPEITLA SESQHIQEDA
ELGTAVALIK THDLDSGFNG EILCQLKGNF PFKIVQDTKN TYRLVTDGAL DREQIPEYNV
TITATDKGNP PLSSSKTITL HILDVNDNVP VFHQASYTVH VAENNPPGAS IAHVRASDPD
LGPNGLVSYY IVASDLEPRE LSSYVSVSAR SGVVFAQRAF DHEQLRAFEL TLQARDQGSP
TLSANVSLRV LVDDRNDNAP LVLYPALGPE GSALFDMVPR SAEPGYLVTK VVAVDADSGY
NAWLSYHIVQ ASEPGLFSLG LRTGEVRTAR TLGDREAARQ RLLVTVRDGG QQPLSATVML
HLIFADSLQE IQPDLSDRPT PSDPQAELQF HLVVALALIS VLFLLAVILA ISLRLRCSSR
PATEGYFQPG VCFKTVPGVL PTYSERTLPY SYNPCAASHS SNTEFKFLNI KAENAAPQDL
LCDEASWFES NDNPEMPSNS GNLQKQAPPN TDWRFSQAQR PGTSGSQNGD DTGTWPNNQF
DTEMLQAMIL ASASEAADGS STLGGGAGTM GLSARYGPQF TLQHVPDYRQ NVYIPGSNAT
LTNAAGKRDG KAPAGGNGNK KKSGKKEKK