ID A0A2K5ERJ2_AOTNA Unreviewed; 1070 AA.
AC A0A2K5ERJ2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Protocadherin 8 {ECO:0000313|Ensembl:ENSANAP00000035839.1};
GN Name=PCDH8 {ECO:0000313|Ensembl:ENSANAP00000035839.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000035839.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000035839.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_012321617.1; XM_012466194.1.
DR AlphaFoldDB; A0A2K5ERJ2; -.
DR STRING; 37293.ENSANAP00000035839; -.
DR Ensembl; ENSANAT00000053908.1; ENSANAP00000035839.1; ENSANAG00000035440.1.
DR GeneID; 105726672; -.
DR GeneTree; ENSGT00940000155219; -.
DR OMA; GESSCHF; -.
DR OrthoDB; 4259465at2759; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
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:0016331; P:morphogenesis of embryonic epithelium; IEA:Ensembl.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
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; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR PANTHER; PTHR24028; CADHERIN-87A; 1.
DR PANTHER; PTHR24028:SF46; PROTOCADHERIN-8; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 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:UP000233020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {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..1070
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014320670"
FT TRANSMEM 750..774
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..135
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 136..245
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 247..354
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 401..497
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 498..609
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 615..723
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 715..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1070 AA; 112885 MW; BCB9E71AE43887FA CRC64;
MSPVRRWGSP CLFPLQLFSL CWVLSVAQSK TVRYSTFEED APGTVIGTLA EDLHMKVSGD
TSFRLMKQFN SSLLRVREGD GQLTVGDAGL DRERLCGQAP QCVLAFDVVS FSQEQFRLVH
VEVEVRDVND HAPRFPRAQI PVEVSEGAAV GTRIPLEVPV DEDVGANGLQ SVRLAEPNSP
FRVELQTRAD GAQCADLVLL QELDRESQAA YSLELVAQDG GRPPRSATAA LSVRVLDAND
HSPAFPQGAV AEVELAEDAP VGSLLLDLDA TDPDEGPNGD VVFAFGARTP PEARRLFRLD
PRSGRLTLAG PVDYERQDTY ELDVRAQDRG PGPRAATCKV IVRIRDVNDN APDIAITPLA
APGAPAASPF AAAVAAAALG GADASSSAGA GTPEAGATSL VPEGAARESL VALVSTSDRD
SGANGQVRCA LYGHEHFRLQ PAYAGSYLVV TAASLDRERI PEYNLTLVAE DRGAPPLRTV
RPYTVRVGDE NDNAPLFTRP VYEVSVRENN PPGAYLATVA ARDRDLGRNG QVTYRLLEAE
VGRAGGAVST YVSVDPATGA IYALRSFDYE TLRQLDVRIQ ASDGGSPQLS SSALVQVRVL
DQNDHAPVLV HPAPANGSLE VAVPGRTAKD TAVARVQARD ADEGANGELA FDLQQQEPRE
AFAIGRRTGE IVLTGDLSQE PPGRVFRALL VISDGGRPPL TTTATVSFVV TAGGGRGPAA
PASAGSPERS RPPGSRLGAS GSALQWDTPL IVIIVLAGSC TLLLAAIIAI ATTCNRRKKE
VRKGGALREE RPGAAGGGAS APGSPEEAAR GAGPRPNMFD VLTFPGSGKA PFGSPAADAP
PPAVAAAEVP GSEGGSATGE SACHFEGQQR LRGAHAEPYG ASPGFGKEPA PPVAVWKGHS
FNTISGREAE KFSGKDSGKG DSDFNDSDSD ISGDALKKDL INHMQSGLWA CTAECKILGH
SDRCWSPSCS GPNAHPSPHP PAQMSTFCKS TSLPRDPLRR DNYYQAQLPK TVGLQSVYEK
VLHRDYDRTV TLLSPPRPGR LPDLQEIGVP LYQSPPGRYL SPKKGANDNV
//
