ID DCBD2_RAT Reviewed; 769 AA.
AC Q91ZV2;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 24-JAN-2024, entry version 113.
DE RecName: Full=Discoidin, CUB and LCCL domain-containing protein 2;
DE AltName: Full=Endothelial and smooth muscle cell-derived neuropilin-like protein;
DE Flags: Precursor;
GN Name=Dcbld2; Synonyms=Esdn;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=11447234; DOI=10.1074/jbc.m105293200;
RA Kobuke K., Furukawa Y., Sugai M., Tanigaki K., Ohashi N., Matsumori A.,
RA Sasayama S., Honjo T., Tashiro K.;
RT "ESDN, a novel neuropilin-like membrane protein cloned from vascular cells
RT with the longest secretory signal sequence among eukaryotes, is up-
RT regulated after vascular injury.";
RL J. Biol. Chem. 276:34105-34114(2001).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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DR EMBL; AF387549; AAL30180.1; -; mRNA.
DR RefSeq; NP_569103.1; NM_130419.1.
DR AlphaFoldDB; Q91ZV2; -.
DR SMR; Q91ZV2; -.
DR STRING; 10116.ENSRNOP00000069998; -.
DR GlyCosmos; Q91ZV2; 5 sites, No reported glycans.
DR GlyGen; Q91ZV2; 5 sites.
DR PhosphoSitePlus; Q91ZV2; -.
DR PaxDb; 10116-ENSRNOP00000002251; -.
DR GeneID; 155696; -.
DR KEGG; rno:155696; -.
DR UCSC; RGD:620543; rat.
DR AGR; RGD:620543; -.
DR CTD; 131566; -.
DR RGD; 620543; Dcbld2.
DR eggNOG; ENOG502QRMB; Eukaryota.
DR InParanoid; Q91ZV2; -.
DR OrthoDB; 5347766at2759; -.
DR PhylomeDB; Q91ZV2; -.
DR PRO; PR:Q91ZV2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0042060; P:wound healing; ISS:UniProtKB.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00057; FA58C; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.170.130.20; LCCL-like domain; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR004043; LCCL.
DR InterPro; IPR036609; LCCL_sf.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR46806:SF3; DISCOIDIN, CUB AND LCCL DOMAIN-CONTAINING PROTEIN 2; 1.
DR PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF03815; LCCL; 1.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00603; LCCL; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF69848; LCCL domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50820; LCCL; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..63
FT /evidence="ECO:0000255"
FT CHAIN 64..769
FT /note="Discoidin, CUB and LCCL domain-containing protein 2"
FT /id="PRO_0000021080"
FT TOPO_DOM 64..523
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..769
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 69..184
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 184..282
FT /note="LCCL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
FT DOMAIN 289..446
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PD2"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 69..96
FT /evidence="ECO:0000250"
FT DISULFID 123..145
FT /evidence="ECO:0000250"
FT DISULFID 212..234
FT /evidence="ECO:0000250"
FT DISULFID 289..446
FT /evidence="ECO:0000250"
SQ SEQUENCE 769 AA; 83915 MW; 5B7936C8FA063A93 CRC64;
MASRAPLRAA RSPQDPGGRA APAATGRAPL PSAGWCPLPP GRNSSSRPRL LLLLLLLLPD
AGAQKGDGCG HTVLGPESGT LTSINYPHTY PNSTVCKWEI RVKTGERIRI KFGDFDIEDS
DYCHLNYLKI FNGIGVSRTE IGKYCGLGLQ MNQSIESKGS EITVLFMSGI HASGRGFLAS
YSVIDKQDLI TCLDTVSNFL EPEFSKYCPA GCLLPFAEIS GTIPHGYRDS SPLCMAGIHA
GVVSDVLGGQ ISVVISKGTP YYESSLANNV TSMVGYLSTS LFTFKTSGCY GTLGMESGVI
ADPQITASSV LEWTDHMGQE NSWKPEKARL RKPGPPWAAF ATDEHQWLQI DLNKEKKITG
IVTTGSTLIE HNYYVSAYRV LYSDDGQKWT VYREPGAAQD KIFQGNKDYH KDVRNNFLPP
IIARFIRVNP VQWQQKIAMK VELLGCQFTL KGRLPKLTQP PPPRNSNNLK NTTVHPKLGR
APKFTQALQP RSRNDLPLLP AQTTATPDVK NTTVTPSVTK DVALAAVLVP VLVMALTTLI
LILVCAWHWR NRKKKAEGTY DLPHWDRAGW WKGVKQLLPA KSVEHEETPV RYSNSEVSHL
SPREVTTVLQ ADSAEYAQPL VGGIVGTLHQ RSTFKPEEGK EASYADLDPY NAPVQEVYHA
YAEPLPVTGP EYATPIVMDM SGHSTASVGL PSTSTFRTAG NQPPALVGTY NTLLSRTDSC
SSGQAQYDTP KGGKPAAAPE ELVYQVPQST QEASGAGRDE KFDAFKETL
//
