THS7A_HUMAN » Thrombospondin type-1 domain-containing protein 7A

THS7A_HUMAN » Thrombospondin type-1 domain-containing protein 7A
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
THS7A_HUMAN » Thrombospondin type-1 domain-containing protein 7A »
Hydrophobic Thickness 31.6 ± 2.2 Å
Tilt Angle 0 ± 2°
ΔGtransfer -41.2 kcal/mol
ΔGfold -21.6 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC
Topology Out
TM Segments 1606-1629 (1600-1632)
Pathways none
PDB none
OPM none
Complexes none
Interactions none
Domains

AA: 198-246, PDBID: 1LSL, Subunit A, Seq Identity:44%, Thrombospondin type 1 domain

AA: 364-416, PDBID: 1VEX, Subunit A, Seq Identity:32%, Thrombospondin type 1 domain

AA: 638-694, PDBID: 5FOE, Subunit B, Seq Identity:36%, Thrombospondin type 1 domain

AA: 775-830, PDBID: 1LSL, Subunit A, Seq Identity:32%, Thrombospondin type 1 domain

AA: 910-960, PDBID: 3OJY, Subunit A, Seq Identity:31%, Thrombospondin type 1 domain

AA: 1039-1093, PDBID: 4OKR, Subunit B, Seq Identity:35%, Thrombospondin type 1 domain

AA: 1100-1150, PDBID: 4OKR, Subunit B, Seq Identity:25%, Thrombospondin type 1 domain

AA: 1169-1219, PDBID: 3GHM, Subunit A, Seq Identity:35%, Thrombospondin type 1 domain

AA: 1290-1340, PDBID: 1LSL, Subunit A, Seq Identity:43%, Thrombospondin type 1 domain

AA: 1344-1392, PDBID: 3T5O, Subunit A, Seq Identity:28%, Thrombospondin type 1 domain

AA: 1418-1474, PDBID: 1LSL, Subunit A, Seq Identity:30%, Thrombospondin type 1 domain

UniProt annotation for THS7A_HUMAN » Thrombospondin type-1 domain-containing protein 7A
FUNCTION: The soluble form promotes endothelial cell migration and filopodia formationduring angiogenesis via a FAK-dependent mechanism.
UniProt features for THS7A_HUMAN » Thrombospondin type-1 domain-containing protein 7A
SIGNAL 1 47 Potential.
CHAIN 48 1657 Thrombospondin type-1 domain-containing protein 7A.
DOMAIN 57 116 TSP type-1 1.
DOMAIN 194 247 TSP type-1 2.
DOMAIN 360 416 TSP type-1 3.
DOMAIN 423 510 TSP type-1 4.
DOMAIN 512 574 TSP type-1 5.
DOMAIN 634 695 TSP type-1 6.
DOMAIN 696 769 TSP type-1 7.
DOMAIN 771 831 TSP type-1 8.
DOMAIN 906 959 TSP type-1 9.
DOMAIN 960 1033 TSP type-1 10.
DOMAIN 1035 1220 TSP type-1 11.
DOMAIN 1221 1284 TSP type-1 12.
DOMAIN 1286 1341 TSP type-1 13.
DOMAIN 1342 1412 TSP type-1 14.
DOMAIN 1414 1475 TSP type-1 15.
COILED 267 315 Potential.
DISULFID 435 505 By similarity.
DISULFID 455 509 By similarity.
DISULFID 466 494 By similarity.
DISULFID 635 677 By similarity.
DISULFID 646 650 By similarity.
DISULFID 689 694 By similarity.
DISULFID 707 764 By similarity.
DISULFID 728 768 By similarity.
DISULFID 739 752 By similarity.
DISULFID 772 814 By similarity.
DISULFID 783 787 By similarity.
DISULFID 824 830 By similarity.
DISULFID 972 1028 By similarity.
DISULFID 994 1032 By similarity.
DISULFID 1005 1018 By similarity.
DISULFID 1036 1073 By similarity.
DISULFID 1047 1051 By similarity.
DISULFID 1213 1219 By similarity.
DISULFID 1287 1325 By similarity.
DISULFID 1298 1302 By similarity.
DISULFID 1335 1340 By similarity.
DISULFID 1351 1407 By similarity.
DISULFID 1358 1411 By similarity.
DISULFID 1369 1388 By similarity.
DISULFID 1415 1459 By similarity.
DISULFID 1426 1430 By similarity.
DISULFID 1469 1474 By similarity.
Amino Acid Sequence for THS7A_HUMAN » Thrombospondin type-1 domain-containing protein 7A
MGLQARRWAS GSRGAAGPRR GVLQLLPLPL PLPLLLLLLL RPGAGRAAAQ GEAEAPTLYL WKTGPWGRCM GDECGPGGIQ TRAVWCAHVE GWTTLHTNCK QAERPNNQQN CFKVCDWHKE LYDWRLGPWN RCQPVISKSL EKPLECIKGE EGIQVREIAC IQKDKDIPAE DIICEYFEPK PLLEQACLIP CQQDCIVSEF SAWSECSKTC GSGLQHRTRH VVAPPQFGGS GCPNLTEFQV CQSSPCEAEE LRYSLHVGPW STCSMPHSRQ VRQARRRGKN KEREKDRSKG VKDPEARELI KKKRNRNRQN RQENKYWDIQ IGYQTREVMC INKTGKAADL SFCQQEKLPM TFQSCVITKE CQVSEWSEWS PCSKTCHDMV SPAGTRVRTR TIRQFPIGSE KECPEFEEKE PCLSQGDGVV PCATYGWRTT EWTECRVDPL LSQQDKRRGN QTALCGGGIQ TREVYCVQAN ENLLSQLSTH KNKEASKPMD LKLCTGPIPN TTQLCHIPCP TECEVSPWSA WGPCTYENCN DQQGKKGFKL RKRRITNEPT GGSGVTGNCP HLLEAIPCEE PACYDWKAVR LGDCEPDNGK ECGPGTQVQE VVCINSDGEE VDRQLCRDAI FPIPVACDAP CPKDCVLSTW STWSSCSHTC SGKTTEGKQI RARSILAYAG EEGGIRCPNS SALQEVRSCN EHPCTVYHWQ TGPWGQCIED TSVSSFNTTT TWNGEASCSV GMQTRKVICV RVNVGQVGPK KCPESLRPET VRPCLLPCKK DCIVTPYSDW TSCPSSCKEG DSSIRKQSRH RVIIQLPANG GRDCTDPLYE EKACEAPQAC QSYRWKTHKW RRCQLVPWSV QQDSPGAQEG CGPGRQARAI TCRKQDGGQA GIHECLQYAG PVPALTQACQ IPCQDDCQLT SWSKFSSCNG DCGAVRTRKR TLVGKSKKKE KCKNSHLYPL IETQYCPCDK YNAQPVGNWS DCILPEGKVE VLLGMKVQGD IKECGQGYRY QAMACYDQNG RLVETSRCNS HGYIEEACII PCPSDCKLSE WSNWSRCSKS CGSGVKVRSK WLREKPYNGG RPCPKLDHVN QAQVYEVVPC HSDCNQYLWV TEPWSICKVT FVNMRENCGE GVQTRKVRCM QNTADGPSEH VEDYLCDPEE MPLGSRVCKL PCPEDCVISE WGPWTQCVLP CNQSSFRQRS ADPIRQPADE GRSCPNAVEK EPCNLNKNCY HYDYNVTDWS TCQLSEKAVC GNGIKTRMLD CVRSDGKSVD LKYCEALGLE KNWQMNTSCM VECPVNCQLS DWSPWSECSQ TCGLTGKMIR RRTVTQPFQG DGRPCPSLMD QSKPCPVKPC YRWQYGQWSP CQVQEAQCGE GTRTRNISCV VSDGSADDFS KVVDEEFCAD IELIIDGNKN MVLEESCSQP CPGDCYLKDW SSWSLCQLTC VNGEDLGFGG IQVRSRPVII QELENQHLCP EQMLETKSCY DGQCYEYKWM ASAWKGSSRT VWCQRSDGIN VTGGCLVMSQ PDADRSCNPP CSQPHSYCSE TKTCHCEEGY TEVMSSNSTL EQCTLIPVVV LPTMEDKRGD VKTSRAVHPT QPSSNPAGRG RTWFLQPFGP DGRLKTWVYG VAAGAFVLLI FIVSMIYLAC KKPKKPQRRQ NNRLKPLTLA YDGDADM