SCAI_HUMAN
ID SCAI_HUMAN Reviewed; 606 AA.
AC Q8N9R8; Q3SXZ1; Q3SXZ2; Q5T163; Q8N1I4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Protein SCAI;
DE AltName: Full=Suppressor of cancer cell invasion protein;
GN Name=SCAI; Synonyms=C9orf126;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [5]
RP FUNCTION, INTERACTION WITH MRTFA AND SRF, AND SUBCELLULAR LOCATION.
RX PubMed=19350017; DOI=10.1038/ncb1862;
RA Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J., Nollau P.,
RA Grosse R.;
RT "SCAI acts as a suppressor of cancer cell invasion through the
RT transcriptional control of beta1-integrin.";
RL Nat. Cell Biol. 11:557-568(2009).
CC -!- FUNCTION: Tumor suppressor which functions to suppress MRTFA-induced
CC SRF transcriptional activity. May function in the RHOA-DIAPH1 signal
CC transduction pathway and regulate cell migration through
CC transcriptional regulation of ITGB1. {ECO:0000269|PubMed:19350017}.
CC -!- SUBUNIT: Interacts with DIAPH1 (By similarity). Forms a nuclear ternary
CC complex with MRTFA and SRF. {ECO:0000250, ECO:0000269|PubMed:19350017}.
CC -!- INTERACTION:
CC Q8N9R8; O14735: CDIPT; NbExp=3; IntAct=EBI-4395514, EBI-358858;
CC Q8N9R8; P27987: ITPKB; NbExp=3; IntAct=EBI-4395514, EBI-751388;
CC Q8N9R8; O15294-3: OGT; NbExp=3; IntAct=EBI-4395514, EBI-11536584;
CC Q8N9R8; Q13526: PIN1; NbExp=3; IntAct=EBI-4395514, EBI-714158;
CC Q8N9R8; Q9BT81: SOX7; NbExp=3; IntAct=EBI-4395514, EBI-7239117;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Nucleus {ECO:0000269|PubMed:19350017}. Cytoplasm
CC {ECO:0000269|PubMed:19350017}. Note=Nuclear localization is required
CC for inhibition of MRTFA. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N9R8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N9R8-2; Sequence=VSP_015120;
CC -!- SIMILARITY: Belongs to the SCAI family. {ECO:0000305}.
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; AK098024; BAC05217.1; -; mRNA.
DR EMBL; AL445930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL451125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87608.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87609.1; -; Genomic_DNA.
DR EMBL; BC104030; AAI04031.1; -; mRNA.
DR EMBL; BC104031; AAI04032.1; -; mRNA.
DR CCDS; CCDS43877.1; -. [Q8N9R8-2]
DR CCDS; CCDS48017.1; -. [Q8N9R8-1]
DR RefSeq; NP_001138349.1; NM_001144877.2. [Q8N9R8-1]
DR RefSeq; NP_775961.2; NM_173690.4. [Q8N9R8-2]
DR AlphaFoldDB; Q8N9R8; -.
DR BioGRID; 130333; 55.
DR IntAct; Q8N9R8; 19.
DR MINT; Q8N9R8; -.
DR STRING; 9606.ENSP00000362650; -.
DR iPTMnet; Q8N9R8; -.
DR PhosphoSitePlus; Q8N9R8; -.
DR BioMuta; SCAI; -.
DR DMDM; 251757332; -.
DR EPD; Q8N9R8; -.
DR jPOST; Q8N9R8; -.
DR MassIVE; Q8N9R8; -.
DR MaxQB; Q8N9R8; -.
DR PaxDb; Q8N9R8; -.
DR PeptideAtlas; Q8N9R8; -.
DR PRIDE; Q8N9R8; -.
DR ProteomicsDB; 72576; -. [Q8N9R8-1]
DR ProteomicsDB; 72577; -. [Q8N9R8-2]
DR Antibodypedia; 7729; 37 antibodies from 16 providers.
DR DNASU; 286205; -.
DR Ensembl; ENST00000336505.11; ENSP00000336756.6; ENSG00000173611.18. [Q8N9R8-1]
DR Ensembl; ENST00000373549.8; ENSP00000362650.4; ENSG00000173611.18. [Q8N9R8-2]
DR GeneID; 286205; -.
DR KEGG; hsa:286205; -.
DR MANE-Select; ENST00000336505.11; ENSP00000336756.6; NM_001144877.3; NP_001138349.1.
DR UCSC; uc004bpd.4; human. [Q8N9R8-1]
DR CTD; 286205; -.
DR DisGeNET; 286205; -.
DR GeneCards; SCAI; -.
DR HGNC; HGNC:26709; SCAI.
DR HPA; ENSG00000173611; Tissue enhanced (lymphoid).
DR MIM; 619222; gene.
DR neXtProt; NX_Q8N9R8; -.
DR OpenTargets; ENSG00000173611; -.
DR PharmGKB; PA165586233; -.
DR VEuPathDB; HostDB:ENSG00000173611; -.
DR eggNOG; ENOG502QPT4; Eukaryota.
DR GeneTree; ENSGT00390000009566; -.
DR HOGENOM; CLU_020095_2_1_1; -.
DR InParanoid; Q8N9R8; -.
DR OMA; MGYDLGG; -.
DR OrthoDB; 346932at2759; -.
DR PhylomeDB; Q8N9R8; -.
DR TreeFam; TF324872; -.
DR PathwayCommons; Q8N9R8; -.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR SignaLink; Q8N9R8; -.
DR BioGRID-ORCS; 286205; 14 hits in 1084 CRISPR screens.
DR ChiTaRS; SCAI; human.
DR GenomeRNAi; 286205; -.
DR Pharos; Q8N9R8; Tbio.
DR PRO; PR:Q8N9R8; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8N9R8; protein.
DR Bgee; ENSG00000173611; Expressed in endothelial cell and 176 other tissues.
DR ExpressionAtlas; Q8N9R8; baseline and differential.
DR Genevisible; Q8N9R8; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR022709; SCAI.
DR InterPro; IPR016607; SCAI_metazoan/Viridiplantae.
DR Pfam; PF12070; SCAI; 1.
DR PIRSF; PIRSF013022; UCP013022; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Signal transduction inhibitor;
KW Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..606
FT /note="Protein SCAI"
FT /id="PRO_0000089735"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..212
FT /note="Necessary to inhibit MRTFA-induced SRF
FT transcriptional activity"
FT /evidence="ECO:0000250"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..173
FT /note="Required for interaction with MRTFA"
FT /evidence="ECO:0000250"
FT MOD_RES 64
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8N2"
FT VAR_SEQ 33
FT /note="R -> SIRGSGDSSHSQSQGERYQHFTEK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_015120"
FT VARIANT 37
FT /note="A -> T (in dbSNP:rs589292)"
FT /id="VAR_023236"
FT CONFLICT 432
FT /note="I -> F (in Ref. 1; BAC05217)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="M -> T (in Ref. 1; BAC05217)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 606 AA; 70399 MW; 08711C37BF37DB96 CRC64;
MVRGARQPQQ PRSRLAPRLT GTVEKPPRKR RSRTEFALKE IMSSGGAEDD IPQGERKTVT
DFCYLLDKSK QLFNGLRDLP QYGQKQWQSY FGRTFDVYTK LWKFQQQHRQ VLDNRYGLKR
WQIGEIASKI GQLYYHYYLR TSETSYLNEA FSFYSAIRQR SYYSQVNKED RPELVVKKLR
YYARFIVVCL LLNKMDVVKD LVKELSDEIE DYTHRFNTED QVEWNLVLQE VAAFIEADPV
MVLNDDNTIV ITSNRLAETG APLLEQGMIV GQLSLADALI IGNCNNQVKF SELTVDMFRM
LQALEREPMN LASQMNKPGM QESADKPTRR ENPHKYLLYK PTFSQLYTFL AASFKELPAN
SVLLIYLSAT GVFPTGRSDS EGPYDFGGVL TNSNRDIING DAIHKRNQSH KEMHCLHPGD
LYPFTRKPLF IIVDSSNSVA YKNFTNLFGQ PLVCLLSPTA YPKALQDQSQ RGSLFTLFLN
NPLMAFLFVS GLSSMRRGLW EKCQEYLRKI NRDIAQLLTH SRSIDQAFLQ FFGDEFLRLL
LTRFIFCSAT MRMHKIFRET RNYPESYPQL PRDETVENPH LQKHILELAS ILDVRNVFFE
NTIDDY
