ID A0A2K6DEV3_MACNE Unreviewed; 519 AA.
AC A0A2K6DEV3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Nectin cell adhesion molecule 1 {ECO:0000313|Ensembl:ENSMNEP00000034438.1};
GN Name=NECTIN1 {ECO:0000313|Ensembl:ENSMNEP00000034438.1};
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:ENSMNEP00000034438.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000034438.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the nectin family.
CC {ECO:0000256|ARBA:ARBA00007810}.
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_011730506.1; XM_011732204.1.
DR AlphaFoldDB; A0A2K6DEV3; -.
DR STRING; 9545.ENSMNEP00000034438; -.
DR Ensembl; ENSMNET00000058888.1; ENSMNEP00000034438.1; ENSMNEG00000040408.1.
DR GeneID; 105476359; -.
DR KEGG; mni:105476359; -.
DR CTD; 5818; -.
DR GeneTree; ENSGT00940000156933; -.
DR OrthoDB; 5358399at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000040408; Expressed in bone marrow and 6 other cell types or tissues.
DR GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR GO; GO:0043296; C:apical junction complex; IEA:Ensembl.
DR GO; GO:0044291; C:cell-cell contact zone; IEA:Ensembl.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0048787; C:presynaptic active zone membrane; IEA:Ensembl.
DR GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0038023; F:signaling receptor activity; IEA:Ensembl.
DR GO; GO:0002934; P:desmosome organization; IEA:Ensembl.
DR GO; GO:0070166; P:enamel mineralization; IEA:Ensembl.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:Ensembl.
DR GO; GO:0006826; P:iron ion transport; IEA:Ensembl.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:1902414; P:protein localization to cell junction; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR CDD; cd05890; IgC1_2_Nectin-1_like; 1.
DR CDD; cd05886; IgV_1_Nectin-1_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR041850; Nectin-1_Ig2.
DR InterPro; IPR041849; Nectin-1_IgV1.
DR PANTHER; PTHR23277:SF69; NECTIN-1; 1.
DR PANTHER; PTHR23277; NECTIN-RELATED; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..519
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014343876"
FT TRANSMEM 358..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..144
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 250..337
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 402..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 57267 MW; 9DFD448A1A3B2647 CRC64;
MARMGLAGAA GRWWGLALGL TAFFLPGAHS QVVQVNDSMY GFIGTDVVLH CSFANPLPSV
KITQVTWQKI TQATNGSKQN VAIYNPSMGV SVLAPYRERV EFLRPSFTDG TIRLSHLELE
DEGVYICEFA TFPTGNRESQ LNLTVMAKPT NWIEGTQAVL RAKKGQDDKV LVATCTSANG
KPPSVVSWET RLKGEAEYQE IRNPNGTVTV ISRYRLVPSR EAHQQSLACI VNYHMDRFKE
SLTLNVQYEP EVTIEGFDGN WYLQRMDVKL TCKADANPPA TEYHWTTLNG SLPKGVEAQN
RTLFFKGPIS YSLAGTYICE ATNPIGTRSG QVEVNITEFP YTPSPPEHGR RAGPVPTAII
GGVAGSVLLV LIVVGGIVVA LRRRRHTFKG DYSTKKHVYG NGYSKAGIPQ HHPPMAQNLQ
YPDDSDDEKK AGPLGGSSYE EEEEEEGGGG GERKVGGPHP KYDEDAKRPY FTVDEAEARQ
DGYGDRTLGY QYDPEQLDLA ENMVSQNDGS FISKKEWYV
//
