ID A0A2K5XAV4_MANLE Unreviewed; 949 AA.
AC A0A2K5XAV4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Protocadherin alpha subfamily C, 2 {ECO:0000313|Ensembl:ENSMLEP00000000466.1};
GN Name=PCDHAC2 {ECO:0000313|Ensembl:ENSMLEP00000000466.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000000466.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000000466.1}
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; A0A2K5XAV4; -.
DR Ensembl; ENSMLET00000001495.1; ENSMLEP00000000466.1; ENSMLEG00000001069.1.
DR GeneTree; ENSGT00940000160554; -.
DR Proteomes; UP000233140; Unplaced.
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:SF68; PROTOCADHERIN ALPHA-11; 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:UP000233140};
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_5014318471"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..133
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 157..242
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 243..349
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 350..454
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 455..564
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 587..677
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 751..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..872
FT /note="Polar residues"
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; 103427 MW; 8BCF87B93658242B CRC64;
MFGFQRRGLG PPRLLLWLLF LEFWEMGSGQ LHYSVYEESK HGTFVGRIAQ DLGLEPAELV
PRLFRVASKT HGDLLEVNLQ NGILFVNSRI DREELCGQSA ECSIHLEVIV DRPLQVFHVN
VEVKDINDNP PVFSLREQKL LIAESKQSDS RFPLEGASDA DIEENALLTY RLSQNEYFSL
DSPTNSKQIK RLSLILKKSL DREKTPELNL LLTATDGGKP ELTGTVQLLV QVLDVNDNDP
EFDKSEYKVS LMENAAKETL VIKLNATDRD EGVNGELTYS LMSVKPNGRP LFTLDQNNGE
VRVNGILDYE ENKFYNIEVQ ATDKGTPPMA GHCTVWVEIL DTNDNSPEVT VTSASLAIRE
DTHPSTVIAL ISVSDRDSGV NGQVTCSLTL HVPFKLVSTF KNYYSLVLDS ALDRESVSAY
DLVVTARDGG SPSLWATARV SVEVADVNDN APAFAQPEYT VFVKENNPPG CHIFTVSARD
ADAQENALVF YSLVERRVGE RALSSYVSVH AESGKVYALQ PLDHEELELL QFQVSARDAG
VPSLGSNVTL QVFVLDENDN APTLLATRAG SAGGAVNELV PRWVGAGHMV TKVRAVDADS
GYNAWLSYEL QPAAVGSRIP FRVGLYTGEI STTRALDEVD SPRHQLLVLV KDHGEPALTA
TATVLVSLVE TGQAPKVSSR ALVAAASPEA ALLDVNVYLI IAICAVSSLL VLTLLLYTAL
RCSVTPTEGT CGPGKPTLVC SRAMGSWSHS QQRQQRVCSG EGPPKTDLMA FSPSLPLGLN
KEEEGERQEP GSNHPGQPRQ PNPDWRYSAS LRAGMHSSVH LEEAGILRAG PGGPDQQWPT
VSSATPEPEA GEVSPPVGAG VNSNSWTFKY GPGNPKQSGP GELPDKFIIP GSPAIISIRQ
EPTNNQIDKS DFITFGKKEE TKKKKKKKKG NKTQEKKEKG NSTTDNSDQ
//