THSD1_HUMAN
ID THSD1_HUMAN Reviewed; 852 AA.
AC Q9NS62; A2A3J3; B2RCF5; Q6P3U1; Q6UXZ2;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
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; ORFNames=UNQ3010/PRO9769;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RA Hiroyama T., Atsushi I., Yukio N., Hiromitsu N.;
RT "Transmembrane molecule with thrombospondin module.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=PNS;
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 [7]
RP INVOLVEMENT IN ANIB12, VARIANTS ANIB12 PHE-5; 450-ARG--ILE-852 DEL;
RP TRP-460; GLY-466; GLU-600; LEU-639; ILE-653 AND PRO-775, CHARACTERIZATION
RP OF VARIANTS ANIB12 PHE-5; 450-ARG--ILE-852 DEL; TRP-460; GLY-466; GLU-600;
RP LEU-639; ILE-653 AND PRO-775, FUNCTION, AND INTERACTION WITH TLN1.
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 [8]
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).
RN [9]
RP INVOLVEMENT IN ANIB12, CHARACTERIZATION OF VARIANTS ANIB12 TRP-460;
RP GLY-466; GLU-600; LEU-639; ILE-653 AND PRO-775, FUNCTION, SUBCELLULAR
RP LOCATION, SUBUNIT, AND INTERACTION WITH TLN1.
RX PubMed=29069646; DOI=10.1159/000484298;
RA Rui Y.N., Xu Z., Fang X., Menezes M.R., Balzeau J., Niu A., Hagan J.P.,
RA Kim D.H.;
RT "The Intracranial Aneurysm Gene THSD1 Connects Endosome Dynamics to Nascent
RT Focal Adhesion Assembly.";
RL Cell. Physiol. Biochem. 43:2200-2211(2017).
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:0000269|PubMed:27895300,
CC ECO:0000269|PubMed:29069646}.
CC -!- SUBUNIT: Part of a complex composed of THSD1, PTK2/FAK1, TLN1 and VCL
CC (PubMed:29069646). Interacts with TLN1 (PubMed:27895300,
CC PubMed:29069646). {ECO:0000269|PubMed:27895300,
CC ECO:0000269|PubMed:29069646}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endosome membrane
CC {ECO:0000269|PubMed:29069646}; Single-pass type I membrane protein
CC {ECO:0000305}. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:29069646}. Note=Localizes to nascent focal
CC adhesions. {ECO:0000269|PubMed:29069646}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Membrane {ECO:0000305}; Single-pass
CC type I membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NS62-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NS62-2; Sequence=VSP_020521;
CC Name=3;
CC IsoId=Q9NS62-3; Sequence=VSP_020522, VSP_020523;
CC -!- DISEASE: Aneurysm, intracranial berry, 12 (ANIB12) [MIM:618734]: A form
CC of cerebral aneurysm, a focal abnormal dilatation of a blood vessel in
CC the brain. Berry intracranial aneurysms, also known as saccular
CC aneurysms, have a characteristic rounded shape and account for the vast
CC majority of intracranial aneurysms. They are the most common cause of
CC non-traumatic subarachnoid hemorrhage, a sudden-onset disease that can
CC lead to severe disability and death. Several risk factors such as
CC smoking, hypertension, and excessive alcohol intake are associated with
CC subarachnoid hemorrhage. {ECO:0000269|PubMed:27895300,
CC ECO:0000269|PubMed:29069646}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AB044385; BAA96553.1; -; mRNA.
DR EMBL; AY358149; AAQ88516.1; -; mRNA.
DR EMBL; AK315087; BAG37552.1; -; mRNA.
DR EMBL; AL359513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471274; EAW55891.1; -; Genomic_DNA.
DR EMBL; CH471274; EAW55894.1; -; Genomic_DNA.
DR EMBL; BC063842; AAH63842.1; -; mRNA.
DR CCDS; CCDS9432.1; -. [Q9NS62-1]
DR CCDS; CCDS9433.1; -. [Q9NS62-2]
DR RefSeq; NP_061146.1; NM_018676.3. [Q9NS62-1]
DR RefSeq; NP_954872.1; NM_199263.2. [Q9NS62-2]
DR AlphaFoldDB; Q9NS62; -.
DR BioGRID; 120988; 2.
DR CORUM; Q9NS62; -.
DR IntAct; Q9NS62; 2.
DR STRING; 9606.ENSP00000258613; -.
DR GlyGen; Q9NS62; 10 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; Q9NS62; -.
DR PhosphoSitePlus; Q9NS62; -.
DR BioMuta; THSD1; -.
DR DMDM; 74752936; -.
DR EPD; Q9NS62; -.
DR jPOST; Q9NS62; -.
DR MassIVE; Q9NS62; -.
DR PaxDb; Q9NS62; -.
DR PeptideAtlas; Q9NS62; -.
DR PRIDE; Q9NS62; -.
DR ProteomicsDB; 82492; -. [Q9NS62-1]
DR ProteomicsDB; 82493; -. [Q9NS62-2]
DR ProteomicsDB; 82494; -. [Q9NS62-3]
DR Antibodypedia; 2452; 235 antibodies from 23 providers.
DR DNASU; 55901; -.
DR Ensembl; ENST00000258613.5; ENSP00000258613.4; ENSG00000136114.17. [Q9NS62-1]
DR Ensembl; ENST00000349258.8; ENSP00000340650.4; ENSG00000136114.17. [Q9NS62-2]
DR Ensembl; ENST00000648254.1; ENSP00000497520.1; ENSG00000136114.17. [Q9NS62-2]
DR GeneID; 55901; -.
DR KEGG; hsa:55901; -.
DR MANE-Select; ENST00000258613.5; ENSP00000258613.4; NM_018676.4; NP_061146.1.
DR UCSC; uc001vgo.4; human. [Q9NS62-1]
DR CTD; 55901; -.
DR DisGeNET; 55901; -.
DR GeneCards; THSD1; -.
DR HGNC; HGNC:17754; THSD1.
DR HPA; ENSG00000136114; Low tissue specificity.
DR MalaCards; THSD1; -.
DR MIM; 616821; gene.
DR MIM; 618734; phenotype.
DR neXtProt; NX_Q9NS62; -.
DR OpenTargets; ENSG00000136114; -.
DR Orphanet; 231160; Familial cerebral saccular aneurysm.
DR Orphanet; 363999; Non-immune hydrops fetalis.
DR PharmGKB; PA134937912; -.
DR VEuPathDB; HostDB:ENSG00000136114; -.
DR eggNOG; ENOG502QY3P; Eukaryota.
DR GeneTree; ENSGT00390000013335; -.
DR HOGENOM; CLU_336470_0_0_1; -.
DR InParanoid; Q9NS62; -.
DR OMA; RNMETWS; -.
DR PhylomeDB; Q9NS62; -.
DR TreeFam; TF333148; -.
DR PathwayCommons; Q9NS62; -.
DR Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR SignaLink; Q9NS62; -.
DR BioGRID-ORCS; 55901; 7 hits in 1064 CRISPR screens.
DR ChiTaRS; THSD1; human.
DR GeneWiki; THSD1; -.
DR GenomeRNAi; 55901; -.
DR Pharos; Q9NS62; Tbio.
DR PRO; PR:Q9NS62; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9NS62; protein.
DR Bgee; ENSG00000136114; Expressed in ventricular zone and 101 other tissues.
DR ExpressionAtlas; Q9NS62; baseline and differential.
DR Genevisible; Q9NS62; HS.
DR GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IMP:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050840; F:extracellular matrix binding; IMP:UniProtKB.
DR GO; GO:0048041; P:focal adhesion assembly; IDA:UniProtKB.
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 Alternative splicing; Cell junction; Disease variant; Disulfide bond;
KW Endosome; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..852
FT /note="Thrombospondin type-1 domain-containing protein 1"
FT /id="PRO_0000249584"
FT TOPO_DOM 25..413
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..852
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 340..393
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 444..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM61"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 80
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 352..387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 356..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 367..377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT VAR_SEQ 341..393
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020521"
FT VAR_SEQ 394..429
FT /note="AFQPSSPSPLQPQGPVKSNNIVTVTGISLCLFIIIA -> GGFSLCCPGWSA
FT VARSWLTTSSASRVHAILLPQPPE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_020522"
FT VAR_SEQ 430..852
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_020523"
FT VARIANT 5
FT /note="L -> F (in ANIB12; loss of function in endothelial
FT cell-matrix adhesion; undetectable protein expression;
FT dbSNP:rs1380388780)"
FT /evidence="ECO:0000269|PubMed:27895300"
FT /id="VAR_083714"
FT VARIANT 125
FT /note="V -> G (in dbSNP:rs13313279)"
FT /id="VAR_027474"
FT VARIANT 224
FT /note="R -> G (in dbSNP:rs9536062)"
FT /id="VAR_027475"
FT VARIANT 450..852
FT /note="Missing (in ANIB12; loss of function in endothelial
FT cell-matrix adhesion)"
FT /evidence="ECO:0000269|PubMed:27895300"
FT /id="VAR_083715"
FT VARIANT 460
FT /note="R -> W (in ANIB12; unknown pathological
FT significance; decreased function in endothelial cell-matrix
FT adhesion; decreased interaction with TLN1;
FT dbSNP:rs776400380)"
FT /evidence="ECO:0000269|PubMed:27895300,
FT ECO:0000269|PubMed:29069646"
FT /id="VAR_083716"
FT VARIANT 466
FT /note="E -> G (in ANIB12; unknown pathological
FT significance; loss of function in endothelial cell-matrix
FT adhesion; decreased interaction with TLN1;
FT dbSNP:rs201805081)"
FT /evidence="ECO:0000269|PubMed:27895300,
FT ECO:0000269|PubMed:29069646"
FT /id="VAR_083717"
FT VARIANT 491
FT /note="D -> H (in dbSNP:rs56013270)"
FT /id="VAR_061920"
FT VARIANT 600
FT /note="G -> E (in ANIB12; unknown pathological
FT significance; loss of function in endothelial cell-matrix
FT adhesion; decreased interaction with TLN1;
FT dbSNP:rs141140186)"
FT /evidence="ECO:0000269|PubMed:27895300,
FT ECO:0000269|PubMed:29069646"
FT /id="VAR_083718"
FT VARIANT 639
FT /note="P -> L (in ANIB12; decreased function in endothelial
FT cell-matrix adhesion; decreased interaction with TLN1;
FT dbSNP:rs1024014523)"
FT /evidence="ECO:0000269|PubMed:27895300,
FT ECO:0000269|PubMed:29069646"
FT /id="VAR_083719"
FT VARIANT 653
FT /note="T -> I (in ANIB12; unknown pathological
FT significance; loss of function in endothelial cell-matrix
FT adhesion; decreased interaction with TLN1;
FT dbSNP:rs371717283)"
FT /evidence="ECO:0000269|PubMed:27895300,
FT ECO:0000269|PubMed:29069646"
FT /id="VAR_083720"
FT VARIANT 768
FT /note="K -> R (in dbSNP:rs9536041)"
FT /id="VAR_027476"
FT VARIANT 775
FT /note="S -> P (in ANIB12; unknown pathological
FT significance; loss of function in endothelial cell-matrix
FT adhesion; decreased interaction with TLN1;
FT dbSNP:rs780150341)"
FT /evidence="ECO:0000269|PubMed:27895300,
FT ECO:0000269|PubMed:29069646"
FT /id="VAR_083721"
SQ SEQUENCE 852 AA; 94584 MW; 597461CFDDC07147 CRC64;
MKPMLKDFSN LLLVVLCDYV LGEAEYLLLR EPGHVALSND TVYVDFQYFD GANGTLRNVS
VLLLEANTNQ TVTTKYLLTN QSQGTLKFEC FYFKEAGDYW FTMTPEATDN STPFPWWEKS
AFLKVEWPVF HVDLNRSAKA AEGTFQVGLF TSQPLCPFPV DKPNIVVDVI FTNSLPEARR
NSRQPLEIRT SKRTELAQGQ WVEFGCAPLG PEAYVTVVLK LLGRDSVITS TGPIDLAQKF
GYKLVMVPEL TCESGVEVTV LPPPCTFVQG VVTVFKEAPR YPGKRTIHLA ENSLPLGERR
TIFNCTLFDM GKNKYCFDFG ISSRSHFSAK EECMLIQRNT ETWGLWQPWS QCSATCGDGV
RERRRVCLTS FPSSPVCPGM SLEASLCSLE ECAAFQPSSP SPLQPQGPVK SNNIVTVTGI
SLCLFIIIAT VLITLWRRFG RPAKCSTPAR HNSIHSPSFR KNSDEENICE LSEQRGSFSD
GGDGPTGSPG DTGIPLTYRR SGPVPPEDDA SGSESFQSNA QKIIPPLFSY RLAQQQLKEM
KKKGLTETTK VYHVSQSPLT DTAIDAAPSA PLDLESPEEA AANKFRIKSP FPEQPAVSAG
ERPPSRLDLN VTQASCAISP SQTLIRKSQA RHVGSRGGPS ERSHARNAHF RRTASFHEAR
QARPFRERSM STLTPRQAPA YSSRTRTCEQ AEDRFRPQSR GAHLFPEKLE HFQEASGTRG
PLNPLPKSYT LGQPLRKPDL GDHQAGLVAG IERTEPHRAR RGPSPSHKSV SRKQSSPISP
KDNYQRVSSL SPSQCRKDKC QSFPTHPEFA FYDNTSFGLT EAEQRMLDLP GYFGSNEEDE
TTSTLSVEKL VI
