SAAL1_MOUSE
ID SAAL1_MOUSE Reviewed; 474 AA.
AC Q9D2C2; Q3UYS6; Q8R2L2;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Protein SAAL1;
DE AltName: Full=Synoviocyte proliferation-associated in collagen-induced arthritis protein 1 {ECO:0000303|PubMed:22127701};
DE Short=SPACIA1;
GN Name=Saal1;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Ovary, Testis, Thymus, and Uterus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 190-474 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Mammary gland;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-14, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-387, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-14, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, Spleen, and Testis;
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=22127701; DOI=10.1002/art.30617;
RA Sato T., Fujii R., Konomi K., Yagishita N., Aratani S., Araya N., Aono H.,
RA Yudoh K., Suzuki N., Beppu M., Yamano Y., Nishioka K., Nakajima T.;
RT "Overexpression of SPACIA1/SAAL1, a newly identified gene that is involved
RT in synoviocyte proliferation, accelerates the progression of synovitis in
RT mice and humans.";
RL Arthritis Rheum. 63:3833-3842(2011).
CC -!- FUNCTION: Plays a role in promoting the proliferation of synovial
CC fibroblasts in response to pro-inflammatory stimuli.
CC {ECO:0000250|UniProtKB:Q96ER3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96ER3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D2C2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D2C2-2; Sequence=VSP_023483;
CC -!- TISSUE SPECIFICITY: Expressed in the synovial tissue of knee joints.
CC {ECO:0000269|PubMed:22127701}.
CC -!- SIMILARITY: Belongs to the SAAL1 family. {ECO:0000305}.
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DR EMBL; AK019878; BAB31898.1; -; mRNA.
DR EMBL; AK030833; BAC27152.1; -; mRNA.
DR EMBL; AK033202; BAC28195.1; -; mRNA.
DR EMBL; AK132193; BAE21024.1; -; mRNA.
DR EMBL; AK134418; BAE22136.1; -; mRNA.
DR EMBL; BC028473; AAH28473.1; -; mRNA.
DR EMBL; BC087944; AAH87944.1; -; mRNA.
DR CCDS; CCDS52253.1; -. [Q9D2C2-1]
DR RefSeq; NP_084509.1; NM_030233.1. [Q9D2C2-1]
DR AlphaFoldDB; Q9D2C2; -.
DR SMR; Q9D2C2; -.
DR BioGRID; 219720; 1.
DR STRING; 10090.ENSMUSP00000120658; -.
DR iPTMnet; Q9D2C2; -.
DR PhosphoSitePlus; Q9D2C2; -.
DR SwissPalm; Q9D2C2; -.
DR EPD; Q9D2C2; -.
DR jPOST; Q9D2C2; -.
DR MaxQB; Q9D2C2; -.
DR PaxDb; Q9D2C2; -.
DR PeptideAtlas; Q9D2C2; -.
DR PRIDE; Q9D2C2; -.
DR ProteomicsDB; 260810; -. [Q9D2C2-1]
DR ProteomicsDB; 260811; -. [Q9D2C2-2]
DR Antibodypedia; 42486; 123 antibodies from 23 providers.
DR Ensembl; ENSMUST00000143082; ENSMUSP00000120658; ENSMUSG00000006763. [Q9D2C2-1]
DR GeneID; 78935; -.
DR KEGG; mmu:78935; -.
DR UCSC; uc009gyu.2; mouse. [Q9D2C2-1]
DR UCSC; uc009gyv.2; mouse. [Q9D2C2-2]
DR CTD; 113174; -.
DR MGI; MGI:1926185; Saal1.
DR VEuPathDB; HostDB:ENSMUSG00000006763; -.
DR eggNOG; ENOG502QS5W; Eukaryota.
DR GeneTree; ENSGT00390000004737; -.
DR HOGENOM; CLU_045694_0_0_1; -.
DR InParanoid; Q9D2C2; -.
DR OMA; CDVVCED; -.
DR PhylomeDB; Q9D2C2; -.
DR TreeFam; TF323873; -.
DR BioGRID-ORCS; 78935; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Saal1; mouse.
DR PRO; PR:Q9D2C2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9D2C2; protein.
DR Bgee; ENSMUSG00000006763; Expressed in ileal epithelium and 183 other tissues.
DR ExpressionAtlas; Q9D2C2; baseline and differential.
DR Genevisible; Q9D2C2; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:1901647; P:positive regulation of synoviocyte proliferation; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..474
FT /note="Protein SAAL1"
FT /id="PRO_0000279541"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 387
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT VAR_SEQ 414..474
FT /note="EKVAQGLKEGQLSKQKCSCAFQSLLPLYGPAVEDFVKVVREVDEALADDLED
FT SFPSVKAQT -> VGGSISDFFSKIKGADYLMS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023483"
SQ SEQUENCE 474 AA; 52769 MW; 08D96FEF6B18B443 CRC64;
MDRNPSPPPP TCGSEDEEDL GGGDRIGSTV YSKHWLFGVL SGLIQIVTPE SGTSGSADEE
EQADLAEEME NEICRVWDMS MDEDVALFLQ EFKAPDIFMG VLAKSPCPRL REICVGILGN
MACFREICES ISKNEDHGQV LLQCLCDSDP PTLLETCRLL LTCLSQTEVA SVWVRRIREH
PSVYANVCFI MSSSTNVDLL VKVGEVVDKL FDLDEKLMLE WIRKGATRLP GQPHEDSEEQ
PVFSIVPCVL EAAKQVRSEN LEGLDVYMRI LQLLTTVDDG VQAIVQCPDT GNDTWRLLFD
LVCHEFCQPD DPPVILQEQK TVLASVFSVL SAISASRAEQ EHLKIEEGDL PLIDSLIRVL
QNMEHCQKKP ENPSESDTEE PTICGPTQDD FHMKILKDIS CEFLSNIFQV LTKEKVAQGL
KEGQLSKQKC SCAFQSLLPL YGPAVEDFVK VVREVDEALA DDLEDSFPSV KAQT
