ID A0A2K6DA14_MACNE Unreviewed; 949 AA.
AC A0A2K6DA14;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Protocadherin alpha subfamily C, 2 {ECO:0000313|Ensembl:ENSMNEP00000032758.1};
GN Name=PCDHAC2 {ECO:0000313|Ensembl:ENSMNEP00000032758.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000032758.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000032758.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A2K6DA14; -.
DR Ensembl; ENSMNET00000057193.1; ENSMNEP00000032758.1; ENSMNEG00000039616.1.
DR GeneTree; ENSGT00940000160554; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000039616; Expressed in cerebellum and 12 other cell types or tissues.
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; IPR031904; Cadherin_CBD.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR PANTHER; PTHR24028; CADHERIN-87A; 1.
DR PANTHER; PTHR24028:SF101; PROTOCADHERIN ALPHA-13; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_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 4: Predicted;
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..949
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014472802"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..133
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 134..242
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 243..350
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 351..455
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 456..565
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 581..678
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 780..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 949 AA; 102605 MW; F35BEEC2917EDF9A CRC64;
MVFSWQGGPR QRQLLLWLLI LAAWETGSGQ LHYSVPEEAK HGTFVGRIAQ DLGLELAELV
PRLFRVASKT HGDLLEVNLQ NGILFVNSRI DREELCGRST ECSIHLEVIV DRPLQVFHVE
VKVRDINDNP PVFPESKKRI TIAESRPPET RFPLDGASDA DIGVNSALTY RLYPNDYFAL
DTQNSRQQMS SLSLILRKTL DREEIQEHSL LLTASDGGKP ELTGTVQLLI TILDVNDNAP
EFYQSVYKVT MLENAFNGTL VIKLNATDPD DGTNGDIVYS FRRPVSPAVV YAFTINPNNG
EIRTKGKLDF EEKKLYEISV EAVDKGNIPM AGHCTLLVEV LDVNDNAPEV TITSLSLPIR
EDTQPSAIIA LISVSDRDSG SNGQVTCTLT PHVPFKLVST YKNYYSLVLD SALDRESVSA
YELVVTARDG GSPSLWATAS VSVGVADVND NAPAFAQPEY TVFVKENNPP GCHIFTASAR
DADAQENALV SYSLVERRVG ERALSSYVSV HAQSGKVYAL QPLDHEELEL LQFQVSALDA
GVPPLGSNVT LQVFVLDEND NAPALLTPGA GSAGGTVSEL VPRSVGAGHV VAKVRAVDAD
SGYNAWLSYE LQPAAVGSRI PFRVGLYTGE ISTTRTLDEV DARRHRLLVL VKDHGEPALT
ATATVLLSLV ESGQQPKASS RASAGAVGQE AALVDVNVYL IIAICAVSSL LVLTLLLYTA
LRCSSPRTEG ACALGKPTLV CSSAVGSWSY SQQRQQRVCS GEGPPKTDLM AFSPSLPPCL
GSAEGTGQRE DSECLKEPRQ PNPDWRYSAS LRAGMHSSVH LEEAGILRAG PGGPDQQWPT
VSSATPEPEA GEVSPPVGAG VNSNSWTFKY GPGNPKQSGP GELPDKFIIP GSPAIISIRQ
EPTNNQIDKS DFITFGKKEE TKKKKKKKKG NKTQEKKEKG NSTTDNSDQ
//
