ID F2TWZ6_SALR5 Unreviewed; 1724 AA.
AC F2TWZ6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Chitin-binding protein {ECO:0000313|EMBL:EGD75905.1};
GN ORFNames=PTSG_00614 {ECO:0000313|EMBL:EGD75905.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL832956; EGD75905.1; -; Genomic_DNA.
DR RefSeq; XP_004998081.1; XM_004998024.1.
DR STRING; 946362.F2TWZ6; -.
DR EnsemblProtists; EGD75905; EGD75905; PTSG_00614.
DR GeneID; 16078677; -.
DR KEGG; sre:PTSG_00614; -.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; F2TWZ6; -.
DR OrthoDB; 1453590at2759; -.
DR Proteomes; UP000007799; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 4.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.10.25.10; Laminin; 8.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 1.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR048287; TSPN-like_N.
DR PANTHER; PTHR24034:SF195; CHITINASE; 1.
DR PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 4.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF00090; TSP_1; 1.
DR SMART; SM00032; CCP; 3.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00179; EGF_CA; 7.
DR SMART; SM00209; TSP1; 2.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 4.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS50923; SUSHI; 1.
DR PROSITE; PS50050; TNFR_NGFR_2; 1.
DR PROSITE; PS50092; TSP1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007799};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1724
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003290061"
FT DOMAIN 293..337
FT /note="TNFR-Cys"
FT /evidence="ECO:0000259|PROSITE:PS50050"
FT REPEAT 293..337
FT /note="TNFR-Cys"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT DOMAIN 634..674
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 718..790
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 830..865
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 940..977
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 978..1019
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1639..1724
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DISULFID 834..844
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 988..1005
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1724 AA; 183047 MW; CB246EF275DE2F19 CRC64;
MRLAVASVVV AAAMLFAAAV TTVPVALAQS DPCSQTCTGD TYEETPCVDP VPSILLDYEA
GVTQPDITVV GDWNEFEQSG DNAFFGFFGD HFYLLNRVRN TGYGMFSFSV DREADYNISI
SYVYFSTSPG AFTDSQRYDV HTDGSRAGTF YIDQQQPPPD GNLTLLGQFH IEQSGYVFLN
ATVKDTSQTT VTASLDAVYI TPADQAVADG SPPVCLPLRV CQDYEYETVA ATATSNRQCA
LVRNCTVSVE YETVAPTATS NRDCATLRTC NATEYETVAP TPTSNRDCAI IEVCADDQYE
TQAPTPTSDR FCDDCDVCDD ATQITDANCT STTNTMCRNI TEPYQYSPWS DWSQSCGTQE
RTRVETCADV KCLDQKPTRQ TRSINGGCDD VCDDTMGQIE CSCTPPSYLI DAYNCSSVYC
DIPTIANATA SATGQLRLDE QALITCSSGY ESVAYGTSFT ITCTEMGLMN DTETCDDVDE
CAVNNGGCAD MCTNLPGTFC CSQDGVYVYS EWSDWSTTCG EGTRTRTRTC NATCGGSCTN
DQPLMETRDI CCPVNANYTY GPFPDWMPTC ARQTRERPES CTASCGGVCT NRINTTQVLT
NGGCEQICNA TSGAIVCDCD PGYRLTSDNA TCEEFNPCDE NNGGCSHTCV AMPLGQFECT
CPSGFEAVDG FNCEDVDECA VNNGGCFQNC NNTAGDYFCS CVDGFMVDPS NSSHCVRINC
ANPPPTLPAS IPSVTARLNG TGPYQFGDEL PYVCEDGFTV DGGAASATSF SLFCRASGMV
DGQFADGCVD VDECSTNNGG CTDGCVNFAG GFNCTCPTGY RLTDGFRCVE INECMEDSPC
DHICTNTAGS FECACRTGFF LETSDNRTCT RVPCGPPPAE QLNATASNSA PAVAVYEDVV
VYNCYDGYTT NGDAGGSSFF FAVCQASGVL SPLVSIACLD VDECLSSPCD QLCDNTLGSF
TCSCLPGYTN TSATTCEDID ECDDPSSCAL DDNTMCVNTD GAFTCECIAG YTRYNNTCQQ
QTHNLLDPLL SSGVVASPTA PQRFADDWVY FDGKGALEIT QPLFIGETFS LTAQVQIVPG
TGGYIFAVTS ATGSTRHFAL YVYELTQRVG VYYRTDSDAS TLAVFQLDSP LDDGALHNIV
LNVQAQSVSL QIDANTTTYT QNLGATISFC DPGPDCKIYI GQRASSAGGA YRLEGIIRHL
RINALSTSDL VPIEDYPSPS AAGPSVIDLL DASNRNVVGS VSADADGALV FDGQSAVVIP
RFHAVPLGAT STFTVTLTVN QDRNTNGYFV AKTDAIGGRF WSLYSSATSN RVSFYYKTSG
STAQQSASFS VSLADGLYHR VMLAVNNATA QLYVDGSLAG TSSLSGRVQD CSPPSSSCIL
QLGRRTDASS SDGLFFLSGA IASASVYSGV FMTADPTAVA PTPALDQQLP ISNASGLAYL
DLLNDTVGFS VGAVRGTEGA TFDGSSRLEV TEHSFSLGPT LSVVGTLRAD TGTAGYIFAK
TSQDGNTRHL ALYMSALSRL TLYYTSTAST SSRNLLFFPD VQLADGVVHS FLLQLVYTAQ
TDTTAVNLYV DGRMQTQQSF QGQLTDCGAR SATCGLAVGQ RLDDNAAGGA FGMTGLIQLL
QLFPHGQLSL ADAPSVSLAS PPYFSVLPAH YIPGQNQGGA YREGVSLEAC ARMCLDDALC
LSFDAGTVGG SMEGSCFLSY VAAGDTGATA LVESSLFAYY ERLS
//