DCBD2_HUMAN
ID DCBD2_HUMAN Reviewed; 775 AA.
AC Q96PD2; B7WNL1; D3DN41; Q8N6M4; Q8TDX2;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Discoidin, CUB and LCCL domain-containing protein 2;
DE AltName: Full=CUB, LCCL and coagulation factor V/VIII-homology domains protein 1;
DE AltName: Full=Endothelial and smooth muscle cell-derived neuropilin-like protein;
DE Flags: Precursor;
GN Name=DCBLD2; Synonyms=CLCP1, ESDN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Coronary artery;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Lung;
RX PubMed=11973641; DOI=10.1038/sj.onc.1205405;
RA Koshikawa K., Osada H., Kozaki K., Konishi H., Masuda A., Tatematsu Y.,
RA Mitsudomi T., Nakao A., Takahashi T.;
RT "Significant up-regulation of a novel gene, CLCP1, in a highly metastatic
RT lung cancer subline as well as in lung cancers in vivo.";
RL Oncogene 21:2822-2828(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 47-775 (ISOFORM 2).
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-606, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC -!- INTERACTION:
CC Q96PD2; P46109: CRKL; NbExp=3; IntAct=EBI-8536103, EBI-910;
CC Q96PD2-2; Q8TB36: GDAP1; NbExp=5; IntAct=EBI-12135455, EBI-11110431;
CC Q96PD2-2; Q13021: MALL; NbExp=3; IntAct=EBI-12135455, EBI-750078;
CC Q96PD2-2; Q5TF39: MFSD4B; NbExp=3; IntAct=EBI-12135455, EBI-11922631;
CC Q96PD2-2; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-12135455, EBI-7545592;
CC Q96PD2-2; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-12135455, EBI-5235586;
CC Q96PD2-2; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-12135455, EBI-6268651;
CC Q96PD2-2; O60636: TSPAN2; NbExp=3; IntAct=EBI-12135455, EBI-3914288;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11973641}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:11973641}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96PD2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96PD2-2; Sequence=VSP_010715;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, heart, skeletal muscle
CC and also in cultured vascular smooth muscle cells.
CC {ECO:0000269|PubMed:11447234, ECO:0000269|PubMed:11973641}.
CC -!- INDUCTION: Increased in lung cancers during the process of tumor
CC progression.
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DR EMBL; AF387547; AAL30178.1; -; mRNA.
DR EMBL; AB073146; BAB91138.1; -; mRNA.
DR EMBL; AC106728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79845.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79847.1; -; Genomic_DNA.
DR EMBL; BC029658; AAH29658.1; -; mRNA.
DR CCDS; CCDS46878.1; -. [Q96PD2-1]
DR RefSeq; NP_563615.3; NM_080927.3. [Q96PD2-1]
DR AlphaFoldDB; Q96PD2; -.
DR SMR; Q96PD2; -.
DR BioGRID; 126285; 62.
DR IntAct; Q96PD2; 24.
DR MINT; Q96PD2; -.
DR STRING; 9606.ENSP00000321573; -.
DR GlyGen; Q96PD2; 6 sites.
DR iPTMnet; Q96PD2; -.
DR PhosphoSitePlus; Q96PD2; -.
DR SwissPalm; Q96PD2; -.
DR BioMuta; DCBLD2; -.
DR DMDM; 57013820; -.
DR EPD; Q96PD2; -.
DR jPOST; Q96PD2; -.
DR MassIVE; Q96PD2; -.
DR MaxQB; Q96PD2; -.
DR PaxDb; Q96PD2; -.
DR PeptideAtlas; Q96PD2; -.
DR PRIDE; Q96PD2; -.
DR ProteomicsDB; 77666; -. [Q96PD2-1]
DR ProteomicsDB; 77667; -. [Q96PD2-2]
DR Antibodypedia; 8135; 211 antibodies from 29 providers.
DR DNASU; 131566; -.
DR Ensembl; ENST00000326840.11; ENSP00000321573.6; ENSG00000057019.16. [Q96PD2-1]
DR Ensembl; ENST00000326857.9; ENSP00000321646.9; ENSG00000057019.16. [Q96PD2-2]
DR GeneID; 131566; -.
DR KEGG; hsa:131566; -.
DR MANE-Select; ENST00000326840.11; ENSP00000321573.6; NM_080927.4; NP_563615.3.
DR UCSC; uc003dtd.4; human. [Q96PD2-1]
DR CTD; 131566; -.
DR DisGeNET; 131566; -.
DR GeneCards; DCBLD2; -.
DR HGNC; HGNC:24627; DCBLD2.
DR HPA; ENSG00000057019; Low tissue specificity.
DR MIM; 608698; gene.
DR neXtProt; NX_Q96PD2; -.
DR OpenTargets; ENSG00000057019; -.
DR PharmGKB; PA134869307; -.
DR VEuPathDB; HostDB:ENSG00000057019; -.
DR eggNOG; ENOG502QRMB; Eukaryota.
DR GeneTree; ENSGT00940000158147; -.
DR HOGENOM; CLU_016654_2_0_1; -.
DR InParanoid; Q96PD2; -.
DR OMA; GVGRTEI; -.
DR OrthoDB; 317808at2759; -.
DR PhylomeDB; Q96PD2; -.
DR TreeFam; TF352191; -.
DR PathwayCommons; Q96PD2; -.
DR SignaLink; Q96PD2; -.
DR BioGRID-ORCS; 131566; 8 hits in 1080 CRISPR screens.
DR ChiTaRS; DCBLD2; human.
DR GeneWiki; DCBLD2; -.
DR GenomeRNAi; 131566; -.
DR Pharos; Q96PD2; Tbio.
DR PRO; PR:Q96PD2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96PD2; protein.
DR Bgee; ENSG00000057019; Expressed in stromal cell of endometrium and 188 other tissues.
DR ExpressionAtlas; Q96PD2; baseline and differential.
DR Genevisible; Q96PD2; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0030522; P:intracellular receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0042060; P:wound healing; IDA:UniProtKB.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00057; FA58C; 1.
DR Gene3D; 2.170.130.20; -; 1.
DR Gene3D; 2.60.120.290; -; 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 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; SSF49785; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR SUPFAM; SSF69848; SSF69848; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50820; LCCL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..66
FT /evidence="ECO:0000255"
FT CHAIN 67..775
FT /note="Discoidin, CUB and LCCL domain-containing protein 2"
FT /id="PRO_0000021078"
FT TOPO_DOM 67..528
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..775
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 72..186
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 187..285
FT /note="LCCL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
FT DOMAIN 292..449
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT REGION 454..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 72..99
FT /evidence="ECO:0000250"
FT DISULFID 126..148
FT /evidence="ECO:0000250"
FT DISULFID 215..237
FT /evidence="ECO:0000250"
FT DISULFID 292..449
FT /evidence="ECO:0000250"
FT VAR_SEQ 574
FT /note="G -> GFYLMVSLACRHNEG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010715"
FT VARIANT 144
FT /note="I -> M (in dbSNP:rs9838238)"
FT /id="VAR_050944"
FT VARIANT 723
FT /note="D -> N (in dbSNP:rs16840208)"
FT /id="VAR_050945"
SQ SEQUENCE 775 AA; 85035 MW; 3D06F81EF2337010 CRC64;
MASRAVVRAR RCPQCPQVRA AAAAPAWAAL PLSRSLPPCS NSSSFSMPLF LLLLLVLLLL
LEDAGAQQGD GCGHTVLGPE SGTLTSINYP QTYPNSTVCE WEIRVKMGER VRIKFGDFDI
EDSDSCHFNY LRIYNGIGVS RTEIGKYCGL GLQMNHSIES KGNEITLLFM SGIHVSGRGF
LASYSVIDKQ DLITCLDTAS NFLEPEFSKY CPAGCLLPFA EISGTIPHGY RDSSPLCMAG
VHAGVVSNTL GGQISVVISK GIPYYESSLA NNVTSVVGHL STSLFTFKTS GCYGTLGMES
GVIADPQITA SSVLEWTDHT GQENSWKPKK ARLKKPGPPW AAFATDEYQW LQIDLNKEKK
ITGIITTGST MVEHNYYVSA YRILYSDDGQ KWTVYREPGV EQDKIFQGNK DYHQDVRNNF
LPPIIARFIR VNPTQWQQKI AMKMELLGCQ FIPKGRPPKL TQPPPPRNSN DLKNTTAPPK
IAKGRAPKFT QPLQPRSSNE FPAQTEQTTA SPDIRNTTVT PNVTKDVALA AVLVPVLVMV
LTTLILILVC AWHWRNRKKK TEGTYDLPYW DRAGWWKGMK QFLPAKAVDH EETPVRYSSS
EVNHLSPREV TTVLQADSAE YAQPLVGGIV GTLHQRSTFK PEEGKEAGYA DLDPYNSPGQ
EVYHAYAEPL PITGPEYATP IIMDMSGHPT TSVGQPSTST FKATGNQPPP LVGTYNTLLS
RTDSCSSAQA QYDTPKAGKP GLPAPDELVY QVPQSTQEVS GAGRDGECDV FKEIL