ID G5BM62_HETGA Unreviewed; 1914 AA.
AC G5BM62;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Thrombospondin-1 {ECO:0000313|EMBL:EHB10292.1};
GN ORFNames=GW7_18700 {ECO:0000313|EMBL:EHB10292.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB10292.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB10292.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
CC -!- SIMILARITY: Belongs to the thrombospondin family.
CC {ECO:0000256|ARBA:ARBA00009456}.
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; JH170984; EHB10292.1; -; Genomic_DNA.
DR STRING; 10181.G5BM62; -.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR InParanoid; G5BM62; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 6.20.200.20; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
DR Gene3D; 4.10.1080.10; TSP type-3 repeat; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR008859; Thrombospondin_C.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR PANTHER; PTHR10199:SF78; THROMBOSPONDIN-1; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF00090; TSP_1; 3.
DR Pfam; PF02412; TSP_3; 7.
DR Pfam; PF05735; TSP_C; 1.
DR Pfam; PF00093; VWC; 1.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00209; TSP1; 3.
DR SMART; SM00210; TSPN; 2.
DR SMART; SM00214; VWC; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57603; FnI-like domain; 1.
DR SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50092; TSP1; 3.
DR PROSITE; PS51234; TSP3; 4.
DR PROSITE; PS51236; TSP_CTER; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00634}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 997..1054
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 1228..1268
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1327..1371
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 1408..1443
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 1467..1502
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 1564..1599
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 1600..1635
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 1639..1853
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1405..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1520..1615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1428
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1522..1549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1584..1615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1914 AA; 211162 MW; 3B83C909EA4E59A4 CRC64;
MSALGLPTIS SRADHKSNSQ IQTTAEIRKT ILLSLGRWQS GEQLREALSE ECGCELKPTG
RAKIATVIKM QKTTVVDKDF STKEIGHYSV TSKTLQMELK KNGTKNRNPQ PEYLQIKEAR
GTLLSQKLMD ASSLQHLNAN RFVLKEKTVN LVIYKQGPGP LDQNTHTAPK RQAVEAPEQT
GEATLAGPRK LESGAPGGGR REAGGGERNP DSPPPLPARP PPIGQRNPQE CARPFKGARL
LRLASSAPSP PQVWAPRGLR VQRPPPAAPA REDSASLGPP SSPLLLLRRH PHRLPAGHKQ
LTMRLAWGLS VLFLVHVCGS NRIPESGGDS SVFDIFELTG AARKGSGRRL VKGPDPSSPA
FRIENANLIP PVPDDKFQDL VDAVRAEKGF LLLASLRQLK KTRGTLLAVE RKDHSGQIFS
VVSNGKAGTL DLSLSVQGKQ QVVSVEEALL ATGQWKSITL FVQEDRAQLY IDCEKMENAE
LDVPIQSIFS RDLASIARLR VAKGDVNDNF QGVLQNVRFV FGTTPEDILR NKGCSSSATN
VLLTLDNTVV NGSSPAIRTN YIGHKTKDLQ AICGISCDEL SSMVLELRRL HTVVTTLQDS
IRKVMEENRQ LVEEVRRPPL CYHNGVQHGN NERWTVDSCT QCHCQLRWHQ TGELGLYLAC
KQSTIYRHPH RLPAGHKQLT MRLAWGLSVL FLVHVCGSNR IPESGGDSSV FDIFELTGAA
RKGSGRRLVK GPDPSSPAFR IENANLIPPV PDDKFQDLVD AVRAEKGFLL LASLRQLKKT
RGTLLAVERK DHSGQIFSVV SNGKAGTLDL SLSVQGKQQV VSVEEALLAT GQWKSITLFV
QEDRAQLYID CEKMENAELD VPIQSIFSRD LASIARLRVA KGDVNDNFQG VLQNVRFVFG
TTPEDILRNK GCSSSATNVL LTLDNTVVNG SSPAIRTNYI GHKTKDLQAI CGISCDELSS
MVLELRRLHT VVTTLQDSIR KVMEENRQLV EEVRRPPLCY HNGVQHGNNE RWTVDSCTQC
HCQNSVTICK KVSCPIMPCS NATVPDGECC PRCWPSDSAD DGWSPWSEWT SCSATCGSGI
QQRGRSCDSL NNRCEGSSVQ TRTCHIQECD KRFKQDGGWS HWSPWSSCSV TCGDGVITRI
RLCNSPSPQM DGKPCEGEAR ETKACRRDPC PISGGWGPWS LWDICSVTCG GGLQTRSRLC
NNPAPQFGGK DCIGDVTESQ VCNKQDCPID GCLSNPCFAG AKCTSYPDGS WKCGACPAGY
SGNGIQCKDV DECREVPDAC FNHNGEHRCK NTDPGYNCLP CPPRFTGTQP YGQGVQHATA
NKQVCKPRNP CTDGTHNCNK NAKCNYLGHY SDPMYRCECK PGYAGNGIIC GEDTDLDGWP
NEDLVCVANA TYHCKKDNCP NLPNSGQEDY DKDGIGDACD EDDDNDKIPD DRDNCPFHYN
PAQYDYDRDD VGDRCDNCPY NHNPDQADTD NNGEGDACAA DIDGDGILNE RDNCQYVYNV
DQRDTDMDGV GDQCDNCPLE HNPDQLDSDS DRIGDTCDNN QDIDEDGHQN NLDNCPYVPN
ANQADHDKDG KGDACDHDDD NDGIPDDRDN CRLVPNPDQK DSDGDGRGDA CKDDFDHDSV
PDIDDICPEN VDISETDFRR FQMIPLDPKG TSQNDPNWVV RHQGKELVQT VNCDPGLAIG
FDEFNAVDFS GTFFINTERD DDYAGFVFGY QSSSRFYVVM WKQVTQSYWD TNPTRAQGYS
GLSVKVVNST TGPGEHLRNA LWHTGNTPGQ VRTLWHDPRH IGWKDFTAYR WRLSHRPKTG
FIRVVMYEGK KIMADSGPIY DKTYAGGRLG LFVFSQEMVF FSDLKYECRA TINKCMQTPA
KGLPTYHWLP RTGTSQKTVR QQHSSGMQQA IILSPGIGAV VSSREKGSMR VLEN
//
