GenomeNet

Database: UniProt
Entry: F7CK30_MONDO
LinkDB: F7CK30_MONDO
Original site: F7CK30_MONDO 
ID   F7CK30_MONDO            Unreviewed;      1681 AA.
AC   F7CK30;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   24-JAN-2024, entry version 87.
DE   SubName: Full=Versican {ECO:0000313|Ensembl:ENSMODP00000025332.4};
GN   Name=VCAN {ECO:0000313|Ensembl:ENSMODP00000025332.4};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000025332.4, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000025332.4, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000025332.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000256|ARBA:ARBA00004498}.
CC   -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC       {ECO:0000256|ARBA:ARBA00006838}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   RefSeq; XP_007487409.1; XM_007487347.2.
DR   STRING; 13616.ENSMODP00000025332; -.
DR   Ensembl; ENSMODT00000025782.4; ENSMODP00000025332.4; ENSMODG00000020252.4.
DR   CTD; 1462; -.
DR   eggNOG; ENOG502QRBE; Eukaryota.
DR   GeneTree; ENSGT00940000156102; -.
DR   HOGENOM; CLU_000303_1_1_1; -.
DR   InParanoid; F7CK30; -.
DR   OMA; DHLDHTQ; -.
DR   OrthoDB; 5323609at2759; -.
DR   TreeFam; TF332134; -.
DR   Proteomes; UP000002280; Chromosome 3.
DR   Bgee; ENSMODG00000020252; Expressed in skeleton of lower jaw and 19 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0072534; C:perineuronal net; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR   GO; GO:0010001; P:glial cell differentiation; IBA:GO_Central.
DR   GO; GO:0002052; P:positive regulation of neuroblast proliferation; IBA:GO_Central.
DR   GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR   CDD; cd00033; CCP; 1.
DR   CDD; cd03588; CLECT_CSPGs; 1.
DR   CDD; cd00054; EGF_CA; 2.
DR   CDD; cd05901; Ig_Versican; 1.
DR   CDD; cd03517; Link_domain_CSPGs_modules_1_3; 1.
DR   CDD; cd03520; Link_domain_CSPGs_modules_2_4; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 3.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR033987; CSPG_CTLD.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR000538; Link_dom.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 1.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF00084; Sushi; 1.
DR   Pfam; PF07686; V-set; 1.
DR   Pfam; PF00193; Xlink; 2.
DR   PRINTS; PR01265; LINKMODULE.
DR   SMART; SM00032; CCP; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00406; IGv; 1.
DR   SMART; SM00445; LINK; 2.
DR   SUPFAM; SSF56436; C-type lectin-like; 3.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS01241; LINK_1; 1.
DR   PROSITE; PS50963; LINK_2; 2.
DR   PROSITE; PS50923; SUSHI; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734};
KW   Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002280};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW   ProRule:PRU00302}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1681
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5023854231"
FT   DOMAIN          13..147
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          151..246
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   DOMAIN          252..348
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   DOMAIN          1374..1410
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1412..1448
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1461..1575
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1579..1639
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   REGION          551..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          737..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          923..946
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1087..1109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1154..1223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1319..1338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1653..1681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1176..1203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1319..1334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1653..1670
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        197..218
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT   DISULFID        295..316
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT   DISULFID        1400..1409
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1438..1447
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1581..1624
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        1610..1637
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   1681 AA;  186964 MW;  FB7439E2593165BC CRC64;
     MLLSIKSVLW MYSTLVVTHA VRQVTVEKSP PVKGFLSGKV SLPCHFSTMP TLPPSYNTTS
     EFLRIKWSKI EEDKSGKDLK ETTVLVAQNG NIKIGQGYKG RVSVPTHPED VGDASLTMVK
     LRASDAGLYR CDVMYGIEDT QDTVSLAVDG VVFHYRAATS RYTLNFEKAQ KACLDNGAVI
     ANPEQLKAAY EDGFEQCDAG WLSDQTVRYP IRAPRAGCYG DMMGKEGVRT YGFRAPHETY
     DVYCYVDHLE GDVFHVTGPN KLTFEEAEEE CANQDARLAT VGELHAAWRN GYDKCDYGWL
     SDASVRHPVT VARAQCGGGL LGVRTLYRFE NQTGFPLPDS KFDAYCYKPK QNISETTTIQ
     LNIPVETEPP NLSKEPQIIP IQATPGIPLI TELPVTQSNI PPMGEIVNIE QKVTVFPYGE
     TKKKFEEATI QPEATVGSST AGSRDSLWYT EYPLSVSGPL EKSDTSEIEE GISLSQPTSS
     ENGVVHNATE LWEKNTEDTQ TQEVITQTEE IEVGPLVTYL ETSGHTPVKE SSTHESLTLS
     TKITMGNKIE KDSTNDFISG SGPTDLYEFP TREDEEQTHT IKPDQNSFPF SQIPEVVTVS
     KISEESNLTL TEYTVSIPTV TGTLTVTLPA KEGSSTDSWE ETQTSGRITE DISGQRVSMP
     LPLENQTEVT FFAPSPDLTS PQGLVEGTPT LIYPDQQTED GEREQVAKPE ATTVHHAIEE
     TEKSMTKDPF YGGIKEEEFS GMKPFPSSPE KTDVTESTDE MTKYFDASMT TTVRTKISVE
     KDIEGKFIST PVNLETVGPP ITTKMEENKT KVHSTGSTLN LEVVTVSKWP LHEDNITSKL
     LTSTEHMGTT ILPTALLTTE KVEQISRFEE PGRDKTSEHF ETGKTFPVTT DVTQRPMVEF
     TEELREDEEE FTESSYSIPK TGIETEPTAK YSPTEEVPSS TGTDRHVVDK TKEGSAFEER
     LELDTPEPVT TVPQFTQTIY GEVPVFVSHS SSTLEPPAHV DATQTVLLIP KPEWEVFTPS
     VSSEGKATQD VHLVDQTPFE ATHSLETIQT ISKTIQLTPV SEKEKPTEYP GFSTGFVATT
     SSELLITPPA EDTDEGDFDG SAYPTSEDEL VTDSKQVTVF KTTAGSREHS ASYPHYISVT
     EHKVKTEVEI VTAATTSEGH LSPRPEQEPE RKASSPSTWE SRTPLSSFTT EGVPQSTQEM
     TAREKEQTSQ DYTELGSGLL ERPKGTETVA LTAVPTVKIT VPSDATTLFS PLDKIHSTST
     SKSFVTKDKP PIIDGEPGEE TISDLVIIDE STYHSTPTPL EDLVTKELET DIDREYFTTS
     SASSIAQTTR QPATEEGKDA LVSQEVSTSE PQARETIHPD INVFIITVTG NKTGRDLCKT
     NPCLNGGTCY TRDTTYVCTC VPGYSGDQCE FDFDECQSNP CRNGATCVDG FNTFTCLCLP
     SYVGALCEQD TETCDYGWHK FQGQCYKYFA HRRTWDAAER ECRLQGAHLT SILSHEEQLF
     VNRVGHDYQW IGLNDKMFEH DFRWTDGSTL QYENWRPNQP DSFFSSGEDC VVIIWHENGQ
     WNDVPCNYHL TYTCKKGTVA CGQPPVVENA KTFGKMKPRY EINSLIRYHC KDGFIQRHLP
     TIRCLGNGRW ALPKITCMNP STYQRTYSKK HFKNSSSAKD NSINSPKHYH RWSSRWQDSR
     R
//
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