ID A0A087R7K3_APTFO Unreviewed; 176 AA.
AC A0A087R7K3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Syndecan {ECO:0000256|RuleBase:RU000649};
DE Flags: Fragment;
GN ORFNames=AS27_02468 {ECO:0000313|EMBL:KFM09457.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM09457.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM09457.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM09457.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell surface proteoglycan. {ECO:0000256|RuleBase:RU000649}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC ECO:0000256|RuleBase:RU000649}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU000649}.
CC -!- SIMILARITY: Belongs to the syndecan proteoglycan family.
CC {ECO:0000256|ARBA:ARBA00005343, ECO:0000256|RuleBase:RU000649}.
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DR EMBL; KL226176; KFM09457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087R7K3; -.
DR STRING; 9233.A0A087R7K3; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:AgBase.
DR GO; GO:1902725; P:negative regulation of satellite cell differentiation; ISS:AgBase.
DR GO; GO:1902723; P:negative regulation of skeletal muscle satellite cell proliferation; ISS:AgBase.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:AgBase.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISS:AgBase.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISS:AgBase.
DR GO; GO:1902766; P:skeletal muscle satellite cell migration; ISS:AgBase.
DR GO; GO:0044319; P:wound healing, spreading of cells; ISS:AgBase.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR001050; Syndecan.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR InterPro; IPR030479; Syndecan_CS.
DR PANTHER; PTHR10915; SYNDECAN; 1.
DR PANTHER; PTHR10915:SF3; SYNDECAN-4; 1.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR PROSITE; PS00964; SYNDECAN; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW ECO:0000256|RuleBase:RU000649};
KW Heparan sulfate {ECO:0000256|ARBA:ARBA00023207,
KW ECO:0000256|RuleBase:RU000649};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974,
KW ECO:0000256|RuleBase:RU000649};
KW Reference proteome {ECO:0000313|Proteomes:UP000053286};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000649};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 124..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 147..165
FT /note="Neurexin/syndecan/glycophorin C"
FT /evidence="ECO:0000259|SMART:SM00294"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM09457.1"
FT NON_TER 176
FT /evidence="ECO:0000313|EMBL:KFM09457.1"
SQ SEQUENCE 176 AA; 19548 MW; 169DA82F0316531B CRC64;
VRETETMDAR WLDYPASGDL PDDEDIGEFR PHLTSDGLDI DEASGSGDYS DSEDAIYLTT
MDTPVMSDNY IPGDTERKIE DEKKNTMMDN EIIPDKAVPV EENLSNKVSM ASTANSSIFE
RTEVLTALIA GGAVGLLFAV FLILLLVYRM KKKDEGSYDL GKKPIYKKAP TNEFYA
//
