THSD1_MOUSE
ID THSD1_MOUSE Reviewed; 851 AA.
AC Q9JM61; Q8C7Q9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Thrombospondin type-1 domain-containing protein 1;
DE AltName: Full=Transmembrane molecule with thrombospondin module;
DE Flags: Precursor;
GN Name=Thsd1; Synonyms=Tmtsp;
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 [MRNA].
RA Hiroyama T., Iwama A., Nakamura Y., Nakauchi H.;
RT "Transmembrane molecule with thrombospondin module.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-462, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=27895300; DOI=10.1161/strokeaha.116.014161;
RA Santiago-Sim T., Fang X., Hennessy M.L., Nalbach S.V., DePalma S.R.,
RA Lee M.S., Greenway S.C., McDonough B., Hergenroeder G.W., Patek K.J.,
RA Colosimo S.M., Qualmann K.J., Hagan J.P., Milewicz D.M., MacRae C.A.,
RA Dymecki S.M., Seidman C.E., Seidman J.G., Kim D.H.;
RT "THSD1 (thrombospondin type 1 domain containing protein 1) mutation in the
RT pathogenesis of intracranial aneurysm and subarachnoid emorrhage.";
RL Stroke 47:3005-3013(2016).
RN [6]
RP ERRATUM OF PUBMED:27895300.
RA Santiago-Sim T., Fang X., Hennessy M.L., Nalbach S.V., DePalma S.R.,
RA Lee M.S., Greenway S.C., McDonough B., Hergenroeder G.W., Patek K.J.,
RA Colosimo S.M., Qualmann K.J., Hagan J.P., Milewicz D.M., MacRae C.A.,
RA Dymecki S.M., Seidman C.E., Seidman J.G., Kim D.H.;
RT "THSD1 (thrombospondin type 1 domain containing protein 1) mutation in the
RT pathogenesis of intracranial aneurysm and subarachnoid emorrhage.";
RL Stroke 48:e240-e240(2016).
CC -!- FUNCTION: Is a positive regulator of nascent focal adhesion assembly,
CC involved in the modulation of endothelial cell attachment to the
CC extracellular matrix. {ECO:0000250|UniProtKB:Q9NS62}.
CC -!- SUBUNIT: Part of a complex composed of THSD1, PTK2/FAK1, TLN1 and VCL.
CC Interacts with TLN1. {ECO:0000250|UniProtKB:Q9NS62}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q9NS62};
CC Single-pass type I membrane protein {ECO:0000305}. Cell junction, focal
CC adhesion {ECO:0000250|UniProtKB:Q9NS62}. Note=Localizes to nascent
CC focal adhesions. {ECO:0000250|UniProtKB:Q9NS62}.
CC -!- TISSUE SPECIFICITY: Expressed in cerebral vascular endothelium.
CC {ECO:0000269|PubMed:27895300}.
CC -!- DISRUPTION PHENOTYPE: Some animals develop hydrocephalus as early as 8
CC weeks after birth. A few die spontaneously at 9 weeks and have diffuse
CC cerebral hemorrhage not seen in wild-type littermates.
CC {ECO:0000269|PubMed:27895300}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC33850.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB039946; BAA92685.1; -; mRNA.
DR EMBL; AK049636; BAC33850.1; ALT_FRAME; mRNA.
DR EMBL; BC119603; AAI19604.1; -; mRNA.
DR CCDS; CCDS22172.1; -.
DR RefSeq; NP_062522.1; NM_019576.2.
DR RefSeq; XP_006509236.1; XM_006509173.3.
DR RefSeq; XP_006509237.1; XM_006509174.3.
DR AlphaFoldDB; Q9JM61; -.
DR SMR; Q9JM61; -.
DR STRING; 10090.ENSMUSP00000067701; -.
DR GlyGen; Q9JM61; 6 sites.
DR iPTMnet; Q9JM61; -.
DR PhosphoSitePlus; Q9JM61; -.
DR PaxDb; Q9JM61; -.
DR PRIDE; Q9JM61; -.
DR ProteomicsDB; 262981; -.
DR GeneID; 56229; -.
DR KEGG; mmu:56229; -.
DR UCSC; uc009lcv.2; mouse.
DR CTD; 55901; -.
DR MGI; MGI:1929096; Thsd1.
DR eggNOG; ENOG502QY3P; Eukaryota.
DR InParanoid; Q9JM61; -.
DR OrthoDB; 130189at2759; -.
DR PhylomeDB; Q9JM61; -.
DR TreeFam; TF333148; -.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR BioGRID-ORCS; 56229; 5 hits in 71 CRISPR screens.
DR PRO; PR:Q9JM61; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JM61; protein.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050840; F:extracellular matrix binding; ISS:UniProtKB.
DR GO; GO:0048041; P:focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
DR Gene3D; 2.20.100.10; -; 1.
DR InterPro; IPR038877; THSD1.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR16311; PTHR16311; 1.
DR Pfam; PF00090; TSP_1; 1.
DR SMART; SM00209; TSP1; 1.
DR SUPFAM; SSF82895; SSF82895; 1.
DR PROSITE; PS50092; TSP1; 1.
PE 1: Evidence at protein level;
KW Cell junction; Disulfide bond; Endosome; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..851
FT /note="Thrombospondin type-1 domain-containing protein 1"
FT /id="PRO_0000249585"
FT TOPO_DOM 25..412
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..851
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 339..392
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 471..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 351..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 355..391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 366..376
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT CONFLICT 625
FT /note="Q -> R (in Ref. 1; BAA92685 and 3; AAI19604)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 851 AA; 94696 MW; 2D157E7253FE902D CRC64;
MKPMLKDFSN LLLVVLCDYV LGEAEYLLLQ EPVHVALSDR TVSVGFHYLS DVNGTLRNVS
VMLWEANTNR TLTTKYLLTN QAQGTLQFEC FYFKEAGDYW FVMIPEVTDN GTQVPLWEKS
AFLKVEWPVF HIDLNRTAKA AEGTFQVGVF TTQPLCLFPV DKPDMLVDVI FTDRLPEARA
SLGQPLEIRA SKRTKLTQGQ WVEFGCAPVG VEAYVTVMLR LLGQDSVIAS TGPIDLAQKF
GYKLMMAPEV TCESVLEVMV LPPPCVFVQG VLAVYKEAPK RPEERTFQVA ENRLPLGERR
TVFNCTLFDV GKNKYCFNFG IVKKGHFSAK ECMLIQRNIE TWGPWQPWSP CSTTCGDAVR
ERRRLCVTSF PSRPSCSGMS SETSPCSLEE CAVFRPPGPS PVSPQDPVKS NNVVTVTGIS
LCLFIIFATV LITLWRRFGR APKCSTPVRH NSIHSPGFRK NSDEENICEL SEPRGSFSDA
GDGPRGSPGD TGIPLTYRCS ASAPPEDEAS GSESFQSNAQ KIIPPLFSYR LAQQQLKEMK
KKGLTETTKV YHVSQSPLTD TVVDATASPP LDLECPEEAA ASKFRIKSPF LDQPGAGTGE
RPPSRLDGIV PPPGCAVSPS QTLIQKSQIR STGGRDGSSE RCHSRSSLFR RTASFHETKQ
SRPFRERSLS ALTPRQVPAY SSRMRTWDQM EDRCRPPSRS THLLPERPEH FQGAGRTSSP
LGPLSKSYTV GHPRRKPDPG DRQAGLVAGA EKMEPHRAHR GPSPSHRSAS RKQSSPIFLK
DSYQKVSQLS PSHFRKDKCQ SFPIHPEFAF YDNTSFRLTE AEQRMLDLPG YFGSNEEDET
TSTLSVEKLV I
