ID   SDC2_BOVIN              Reviewed;         202 AA.
AC   Q58DD4; Q2KIX8;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Syndecan-2;
DE            Short=SYND2;
DE   AltName: CD_antigen=CD362;
DE   Flags: Precursor;
GN   Name=SDC2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell surface proteoglycan that bears heparan sulfate.
CC       Regulates dendritic arbor morphogenesis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via cytoplasmic domain) with SARM1. Forms a complex
CC       with SDCBP and PDCD6IP. {ECO:0000250|UniProtKB:P34741,
CC       ECO:0000250|UniProtKB:P43407}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
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DR   EMBL; BT021663; AAX46510.1; -; mRNA.
DR   EMBL; BC112468; AAI12469.1; -; mRNA.
DR   RefSeq; NP_001029960.2; NM_001034788.2.
DR   AlphaFoldDB; Q58DD4; -.
DR   STRING; 9913.ENSBTAP00000019090; -.
DR   PaxDb; Q58DD4; -.
DR   PeptideAtlas; Q58DD4; -.
DR   PRIDE; Q58DD4; -.
DR   Ensembl; ENSBTAT00000019090; ENSBTAP00000019090; ENSBTAG00000014357.
DR   GeneID; 615785; -.
DR   KEGG; bta:615785; -.
DR   CTD; 6383; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014357; -.
DR   VGNC; VGNC:34379; SDC2.
DR   eggNOG; ENOG502RZ6V; Eukaryota.
DR   GeneTree; ENSGT00940000157222; -.
DR   HOGENOM; CLU_046599_2_1_1; -.
DR   InParanoid; Q58DD4; -.
DR   OMA; ASASGSX; -.
DR   OrthoDB; 1362808at2759; -.
DR   TreeFam; TF320463; -.
DR   Proteomes; UP000009136; Chromosome 14.
DR   Bgee; ENSBTAG00000014357; Expressed in liver and 105 other tissues.
DR   ExpressionAtlas; Q58DD4; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0048813; P:dendrite morphogenesis; IBA:GO_Central.
DR   GO; GO:0048814; P:regulation of dendrite morphogenesis; ISS:UniProtKB.
DR   InterPro; IPR003585; Neurexin-like.
DR   InterPro; IPR001050; Syndecan.
DR   InterPro; IPR031201; Syndecan-2.
DR   InterPro; IPR027789; Syndecan/Neurexin_dom.
DR   InterPro; IPR030479; Syndecan_CS.
DR   PANTHER; PTHR10915; PTHR10915; 1.
DR   PANTHER; PTHR10915:SF6; PTHR10915:SF6; 1.
DR   Pfam; PF01034; Syndecan; 1.
DR   SMART; SM00294; 4.1m; 1.
DR   PROSITE; PS00964; SYNDECAN; 1.
PE   2: Evidence at transcript level;
KW   Differentiation; Glycoprotein; Heparan sulfate; Membrane; Neurogenesis;
KW   Phosphoprotein; Proteoglycan; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..202
FT                   /note="Syndecan-2"
FT                   /id="PRO_0000227542"
FT   TOPO_DOM        23..148
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        170..202
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          41..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..130
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            143..144
FT                   /note="Cleavage of ectodomain"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         188
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P34741"
FT   CARBOHYD        41
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        55
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        57
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        125
FT                   /note="A -> D (in Ref. 2; AAI12469)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   202 AA;  22399 MW;  7E855A0BFFA65B86 CRC64;
     MRRAWILLTW VLVACVSAES RAELTSDKDM YLDNNSIEEA SGVYPIDDDD YASASGSGAG
     EDGESPELTT SRPIPKIPFT STAPRVETTT LSKIQDKIPA QTKSPEEIDK EKVHLPDSER
     KTDPAEEDTN VYTEKHSDNL FKRTEVLAAV IAGGVIGFLF AIFLILLLVY RMRKKDEGSY
     DLGERKPSSA AYQKAPTKEF YA