ID H2TNK8_TAKRU Unreviewed; 1207 AA.
AC H2TNK8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 24-JAN-2024, entry version 85.
DE SubName: Full=Neurocan core protein-like {ECO:0000313|Ensembl:ENSTRUP00000026264.3};
GN Name=LOC101063313 {ECO:0000313|Ensembl:ENSTRUP00000026264.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000026264.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000026264.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000026264.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; H2TNK8; -.
DR Ensembl; ENSTRUT00000026371.3; ENSTRUP00000026264.3; ENSTRUG00000010430.3.
DR GeneTree; ENSGT00940000158649; -.
DR InParanoid; H2TNK8; -.
DR OMA; FDWGESL; -.
DR Proteomes; UP000005226; Chromosome 22.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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 CDD; cd00033; CCP; 1.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd03517; Link_domain_CSPGs_modules_1_3; 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; 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 PANTHER; PTHR22804:SF41; BREVICAN CORE PROTEIN; 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 4: Predicted;
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1207
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025579191"
FT DOMAIN 47..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..345
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 903..939
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 941..977
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 990..1104
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1108..1168
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 372..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1194
FT /note="Basic 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 929..938
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 967..976
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1110..1153
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1139..1166
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1207 AA; 131526 MW; 11D44F15B4127A6A CRC64;
MALRAAAQQI LLIMMLLISL GSATAVVNMR RITRPPVQQM LAGRAILPCV FTLQTNSSDQ
PPFLLWTHSR IPAGGKGSPE EQVVLSAKGD VIKVNKAFSG RVMLPGYAAN PLNATMEISS
LRSNDSGTYH CQVVMDNDYE RDTVPLVVSG VVFHYQAPGA HYALSFTDAQ RACREMSAQM
AAPAQLWAAY YDGFASCAAG WLDDQTVRYS VQLPELGCYG HKEYSAGVRN YGKKDPKELF
DVYCFAQELD GEVFHSSVPG RLSLSSASDR CVSLGGQLAT VGQLYLAWKA GLDSCAPGWL
SDGSVRYPVT WPRPDCGGSW PGVHAVTLNN THDNATALYD AYCYRGKVQT SDPISQIYSS
LWKPWSYLTG SSEAKPAGTD DPDVTSQTTS IKGSTETSGD VLPSNWTGLV DLEEEETNPS
ANASSDPWSS ESSGSFLTLH LIPGQNWFDW GESLEPGLGS EEFLRPLVNP TPAEKKAILK
IVSSISKPWN YLLGTEDETE APDKAPTSRS GGAKEPTTKT ADESDSSTLS GLFSWGSSWF
TAPARENSTP ASEDSSTRLG STSDASDNPT MVESNKSLEN SEWHTFTPFS SAGAVASVGG
VSVETQTTVL PEAVTTSHRR TSGRGRGRGR KYKGEDRSRG EDKVRGETEG SGEIAGVEAK
GEIQVSRRPV GTSKPRERSR ERSRERGHRR GQFTTTTAAA PTTNAQELTS MTTTVSEGTD
VSTSESTSAS PTEAPSSAPM QSLFITTSLS PSPRSPSKSL LESQSPSASP SEAIPFSFSV
FPATSSSSHD SPTSFLSSSP TSIFSDSSSQ TVGSGDPSLS PLPDNQDSST KPHTSLRWVP
LESAVLNSSL DYPPLLPVAA DEEEPAWSHA VGSGALLPGN LEEESSRGGA NISTTSSLGP
TVEVDPCVTN PCLHGGKCLP QGTGYSCYCP QGYAGENCEI DVDDCQSEPC ENGGTCIDKI
DSFLCLCLPS YEGDRCEKDI EGCEHGWRKF HGHCYRYFTH RHTWEDAEKD CREHSAHLSS
IISATEQEFI NGLGHDNAWI GLNDRTVEED FQWTDNTDLV YENWRENQPD NFFAGGEDCA
VTIAHEEGKW NDVPCNYNLP YICKKGTVLC GTPPVVENTH LIGRRRSHYD IHAVVRYQCT
EGFFQRHIPT IRCRADGSWE RPRIICAKSR RSHRYRRHRH SQHRERRIHR RHGGEGHRAR
EDAHSYY
//