ID   Q59H32_HUMAN            Unreviewed;       961 AA.
AC   Q59H32;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   13-SEP-2023, entry version 99.
DE   SubName: Full=Protocadherin gamma subfamily A, 3 isoform 1 variant {ECO:0000313|EMBL:BAD92164.1};
DE   Flags: Fragment;
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 {ECO:0000313|EMBL:BAD92164.1};
RN   [1] {ECO:0000313|EMBL:BAD92164.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:BAD92164.1};
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RT   "Homo sapiens protein coding cDNA.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00003436}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   EMBL; AB208927; BAD92164.1; -; mRNA.
DR   AlphaFoldDB; Q59H32; -.
DR   PeptideAtlas; Q59H32; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
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   CDD; cd11304; Cadherin_repeat; 6.
DR   Gene3D; 2.60.40.60; Cadherins; 6.
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   PANTHER; PTHR24028; CADHERIN-87A; 1.
DR   PANTHER; PTHR24028:SF234; PROTOCADHERIN GAMMA-A3; 1.
DR   Pfam; PF00028; Cadherin; 4.
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; Cadherin-like; 6.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 6.
PE   2: Evidence at transcript level;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW   ProRule:PRU00043}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|SAM:Phobius}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        718..743
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          57..162
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          163..271
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          272..376
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          377..481
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          482..591
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          608..711
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   REGION          834..870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          931..961
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        835..870
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAD92164.1"
SQ   SEQUENCE   961 AA;  104536 MW;  B0BB55883E84BCD2 CRC64;
     KTSFLEKIRL ESVVGNWNRI QRKRFTEKEM TNCLSFRNGR GLALLCALLG TLCETGSGQI
     RYSVSEELDK GSFVGNIAND LGLEPRELAE RGVRIVSRGR TQLFSLNSQS GSLVTAERID
     REELCAQIPL CLVKINILVE DKLKIFEVEI EIKDINDNAP NFPTEELEIK IGELTVPGTR
     FPIKTAFDPD VGINSLQNYK LSPNDYFSLA VNSVSEGAKY PELVLERALD REKKEIHQLV
     LVASDGGDPV HSGNLHIQVI VLDANDNPPM FTQPEYRVSV WENVPVGTRL LTVNATDPDE
     GFNAQVSYIL DKMPGKIAEI FHLNSVSGEV SILKSLDYED AMFYEIKIEA QDGPGLLSRA
     KILVTVLDVN DNAPEITITS LTSSVPEEGT VGREIALIDV HDRDSGQNGQ VEVFVLGNLP
     FKLEKSIDQY YRLVTATSLD REQISEYNIS LRASDGGSPP LSTETHITLH VIDINDNPPT
     FPHLSYSAYI PENNPRGASI FSVTAQDPDS NNNARITYAL TEDTLQGAPL SSFVSINSNT
     GVLYALRSFD YEQFRDLKLL VTASDSGNPP LSSNVSLNLF VLDQNDNAPE ILYPALPTDG
     STGVELAPRS AEPGYLVTKV VAVDRDSGQN AWLSYRLLKA SEPGLFSVGL HTGEVRTARA
     LLDRDALKQS LVVAVQDHGQ PPLSATVTLT VAVADRIPDI LADLGSLEPS AKPNDSDLTL
     YLVVAVAAVS CVFLAFVIVL LALRLRRWHK SRLLQASGGG LASTPGSHFV GADGVRAFLQ
     TYSHEVSLTA DSRKSHLIFP QPNYADTLIS QESCEKSEPL LITQDLLEMK GDSNLLQQAP
     PNTDWRFSQA QRPGTSGSQN GDDTGTWPNN QFDTEMLQAM ILASASEAAD GSSTLGGGAG
     TMGLSARYGP QFTLQHVPDY RQNVYIPGSN ATLTNAAGKR DGKAPAGGNG NKKKSGKKEK
     K
//