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Database: UniProt
Entry: A0A2K5XAV4_MANLE
LinkDB: A0A2K5XAV4_MANLE
Original site: A0A2K5XAV4_MANLE 
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
//
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