THS7B_MOUSE
ID THS7B_MOUSE Reviewed; 1607 AA.
AC Q6P4U0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Thrombospondin type-1 domain-containing protein 7B {ECO:0000305};
DE Flags: Precursor;
GN Name=Thsd7b {ECO:0000312|MGI:MGI:2443925};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
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DR EMBL; BC063250; AAH63250.1; -; mRNA.
DR CCDS; CCDS15255.1; -.
DR RefSeq; NP_766073.2; NM_172485.3.
DR AlphaFoldDB; Q6P4U0; -.
DR STRING; 10090.ENSMUSP00000073220; -.
DR GlyConnect; 2768; 3 N-Linked glycans (2 sites).
DR GlyGen; Q6P4U0; 14 sites, 3 N-linked glycans (2 sites).
DR iPTMnet; Q6P4U0; -.
DR PhosphoSitePlus; Q6P4U0; -.
DR PaxDb; Q6P4U0; -.
DR PRIDE; Q6P4U0; -.
DR ProteomicsDB; 258875; -.
DR Antibodypedia; 62318; 9 antibodies from 5 providers.
DR DNASU; 210417; -.
DR Ensembl; ENSMUST00000073527; ENSMUSP00000073220; ENSMUSG00000042581.
DR GeneID; 210417; -.
DR KEGG; mmu:210417; -.
DR UCSC; uc007clv.2; mouse.
DR CTD; 80731; -.
DR MGI; MGI:2443925; Thsd7b.
DR VEuPathDB; HostDB:ENSMUSG00000042581; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000159262; -.
DR HOGENOM; CLU_004819_0_0_1; -.
DR InParanoid; Q6P4U0; -.
DR OMA; PCKINNE; -.
DR OrthoDB; 20284at2759; -.
DR PhylomeDB; Q6P4U0; -.
DR TreeFam; TF329791; -.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR BioGRID-ORCS; 210417; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Thsd7b; mouse.
DR PRO; PR:Q6P4U0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6P4U0; protein.
DR Bgee; ENSMUSG00000042581; Expressed in trigeminal ganglion and 127 other tissues.
DR ExpressionAtlas; Q6P4U0; baseline and differential.
DR Genevisible; Q6P4U0; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IBA:GO_Central.
DR Gene3D; 2.20.100.10; -; 11.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR044004; TSP1_spondin_dom.
DR Pfam; PF19028; TSP1_spondin; 4.
DR Pfam; PF00090; TSP_1; 5.
DR SMART; SM00209; TSP1; 15.
DR SUPFAM; SSF82895; SSF82895; 13.
DR PROSITE; PS50092; TSP1; 13.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..1607
FT /note="Thrombospondin type-1 domain-containing protein 7B"
FT /id="PRO_0000260252"
FT TOPO_DOM 32..1556
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1557..1577
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1578..1607
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 40..98
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 102..177
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 179..233
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 336..392
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 399..482
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 484..543
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 601..661
FT /note="TSP type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 662..735
FT /note="TSP type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 737..796
FT /note="TSP type-1 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 797..869
FT /note="TSP type-1 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 871..924
FT /note="TSP type-1 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 925..999
FT /note="TSP type-1 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1001..1126
FT /note="TSP type-1 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1128..1182
FT /note="TSP type-1 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1183..1246
FT /note="TSP type-1 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1248..1303
FT /note="TSP type-1 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1304..1369
FT /note="TSP type-1 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1371..1432
FT /note="TSP type-1 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 683
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 757
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 842
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 933
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 985
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 411..477
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 431..481
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 442..466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 602..643
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 613..617
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 655..660
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 738..779
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 749..753
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 789..795
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 937..994
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 960..998
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 971..984
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1002..1039
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1013..1017
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1121..1125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1249..1287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1260..1264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1297..1302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1372..1416
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1383..1387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1426..1431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ SEQUENCE 1607 AA; 179309 MW; AAD38F2EF5E81036 CRC64;
MFLRSDLAVT HWVSRSMRKL FLVLSLLLSQ AAHLEGRKDN QFLWKTGPWG RCAGDCGPGG
AQSRAVWCFH IEGWTSPMSN CDESSQPPKE RSCFRVCDWH SDLFQWEVSD WHRCLLVPGA
QGEPRPRAVE CVTAQHGLQH RTVRCLQKLN RTMVSNEICE HFAPQPPTEQ ACLIPCPRDC
VVSEFSPWST CPEGCGKKLQ HRTRVAIAPP LYGGLQCPNL TESRACEAPV SCPLGKEEYS
FSLKVGPWSK CRLPHLKEVD LSGRNIQDFS SDSNEQVTLT HQSYKAHHHS QPGDVVIGFQ
TRQVWCTRSD GRNALLSLCV RDSFPLTVQP CVMPKDCETS EWSPWSPCSK TCRSGTLSPG
VRSRSRNVKH IAIGGGQECP ELLEKETCIA EGEFLQPCPR YSWRTSEWKE CQVSLLLEQH
DPLWHETGPI CGGGIQTREV YCAQSLPATI ASRTKEVSRP VERTLCLGPA PSASQLCNVP
CSMDCIVSSW STWGPCVFEN CHDPQGKKGF RMRQRHVLME STGPMGRCPH LAESVPCEDP
MCHRWLASEG ICIADHGKCG LGHRILKAVC QNERGEEVSG GLCPVPPPPE RMACEIPCRM
DCVVSEWTVW SSCSQSCSNK NSDGKQTRSR SILALAGEGG KTCPSSQELQ EYRLCNDHSC
TQLYWETSAW GSCSENTLVT ALNVTIGWNG EATCGVGIQT RKVFCIKSHV GQVMTKRCPE
STRPETVRPC FLPCKKDCLV TAFSEWTPCP RPCQPGNTTI KQSRYRIIIQ EAANGGQECP
DTLFEERECE DISLCPSYRW KPQKWSSCIL VPESIRQGRT GTSEACGKGL QTRAVSCISD
DNQSAEMTEC LKQMNGMPPL VQECTIPCRD DCTFTPWSKF TPCSKNCEAT QIRRRQLTGK
SRKKEKCQDA SLYPLVEMEP CPCDTFMSHP YGNWSACILP EGKRDAQQGG LWVQGDDKEC
GEGVRFRAIA CSNINGRPVD PSFCNSSGYI QEACVIPCPF DCKLSDWSSW GSCSSSCGIG
VRIRSKWLKE KPYSGGRPCP KLDLKNQVHE AVPCYSECDQ YSWVVEHWSP CKINNELRSP
RCGRGTQSRR IRCVSTADRE GGAVNRSLCN QDDAPQETQA CSLLCPSECV MSEWGTWSRC
PQSCDPHAMQ RRTRHLLRPS LNSRTCGEDS QVRPCLLNEN CFQFQYNLTE WSTCQLSENV
SCGQGVRTRL LSCVRSDGKS VSMDHCEQRN LEKPQRMSIP CLVECVVNCQ LSGWTTWTEC
SQTCGQGGRM SRTRFIIMPT QGEGRQCPTE LTQQKPCPVT PCYSWVLGNW SACKLEGGDC
GEGVQVRSFS CVVHNGSISH TAVPVEEALC GEVPFQEGIL KQLCSVPCPG DCHITPWSEW
SKCELTCIDG RSFETTGRQS RSRTFIIQSF ENQDSCPQQV LETRPCTGGK CYHYIWKASL
WNNNERTVWC QRSDGLNVTG GCSPQARPAA IRQCIPACKK PFSYCTQGGV CGCEKGYTEI
MRSSGFLDYC MKVPGSEDKK ADVKNLSGKN RPVNSKIHDI FKGWSLQPLD PDGRVKMWVY
GVSGGSFLIM IFLVFTSYLV CKKPKPHQST PRHQKPLTLA YDGDLDM
