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   02-SEP-2026, entry version 175.
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_080927.4. [Q96PD2-1]
DR   AlphaFoldDB; Q96PD2; -.
DR   SMR; Q96PD2; -.
DR   BioGRID; 126285; 71.
DR   FunCoup; Q96PD2; 662.
DR   IntAct; Q96PD2; 50.
DR   MINT; Q96PD2; -.
DR   STRING; 9606.ENSP00000321573; -.
DR   GlyCosmos; Q96PD2; 6 sites, No reported glycans.
DR   GlyGen; Q96PD2; 8 sites, 6 N-linked glycans (4 sites), 1 O-linked glycan (2 sites).
DR   iPTMnet; Q96PD2; -.
DR   PhosphoSitePlus; Q96PD2; -.
DR   SwissPalm; Q96PD2; -.
DR   BioMuta; DCBLD2; -.
DR   DMDM; 57013820; -.
DR   jPOST; Q96PD2; -.
DR   MassIVE; Q96PD2; -.
DR   PaxDb; 9606-ENSP00000321573; -.
DR   PeptideAtlas; Q96PD2; -.
DR   ProteomicsDB; 77666; -. [Q96PD2-1]
DR   ProteomicsDB; 77667; -. [Q96PD2-2]
DR   Pumba; Q96PD2; -.
DR   Antibodypedia; 8135; 237 antibodies from 32 providers.
DR   DNASU; 131566; -.
DR   Ensembl; ENST00000326840.11; ENSP00000321573.6; ENSG00000057019.17. [Q96PD2-1]
DR   Ensembl; ENST00000326857.9; ENSP00000321646.9; ENSG00000057019.17. [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   AGR; HGNC:24627; -.
DR   ClinPGx; PA134869307; -.
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   OpenTargets; ENSG00000057019; -.
DR   VEuPathDB; HostDB:ENSG00000057019; -.
DR   eggNOG; ENOG502QRMB; Eukaryota.
DR   GeneTree; ENSGT00940000158147; -.
DR   HOGENOM; CLU_016654_2_0_1; -.
DR   InParanoid; Q96PD2; -.
DR   OMA; DACHFNY; -.
DR   OrthoDB; 441660at2759; -.
DR   PAN-GO; Q96PD2; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; Q96PD2; -.
DR   PathwayCommons; Q96PD2; -.
DR   SignaLink; Q96PD2; -.
DR   SIGNOR; Q96PD2; -.
DR   Agora; ENSG00000057019; -.
DR   BioGRID-ORCS; 131566; 8 hits in 1160 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 189 other cell types or tissues.
DR   ExpressionAtlas; Q96PD2; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005886; C: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   FunFam; 2.60.120.260:FF:000002; Coagulation factor VIII; 1.
DR   FunFam; 2.170.130.20:FF:000002; Discoidin, CUB and LCCL domain-containing protein 2; 1.
DR   FunFam; 2.60.120.290:FF:000035; Discoidin, CUB and LCCL domain-containing protein 2; 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; IPR050633; Neuropilin_MCO_CoagFactor.
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   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
KW   Phosphoprotein; Proteomics identification; Reference proteome; Signal;
KW   Transmembrane; 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        468..477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..517
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..706
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
//