ALS_MOUSE
ID ALS_MOUSE Reviewed; 603 AA.
AC P70389; Q9DBI7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 167.
DE RecName: Full=Insulin-like growth factor-binding protein complex acid labile subunit;
DE Short=ALS;
DE Flags: Precursor;
GN Name=Igfals; Synonyms=Albs, Als;
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 [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=8816745; DOI=10.1073/pnas.93.19.10028;
RA Boisclair Y.R., Seto D., Hsieh S., Hurst K.R., Ooi G.T.;
RT "Organization and chromosomal localization of the gene encoding the mouse
RT acid labile subunit of the insulin-like growth factor binding complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10028-10033(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Lung, and Spleen;
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).
CC -!- FUNCTION: May have an important role in regulating the access of
CC circulating IGFs to the tissues.
CC -!- SUBUNIT: Forms a ternary complex of about 140 to 150 kDa with IGF-I or
CC IGF-II and IGFBP-3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
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DR EMBL; U66900; AAB17270.1; -; Genomic_DNA.
DR EMBL; AK004926; BAB23677.1; -; mRNA.
DR CCDS; CCDS37497.1; -.
DR PIR; JC6128; JC6128.
DR RefSeq; NP_032366.2; NM_008340.3.
DR AlphaFoldDB; P70389; -.
DR SMR; P70389; -.
DR BioGRID; 200551; 1.
DR IntAct; P70389; 1.
DR MINT; P70389; -.
DR STRING; 10090.ENSMUSP00000060169; -.
DR GlyGen; P70389; 7 sites.
DR iPTMnet; P70389; -.
DR PhosphoSitePlus; P70389; -.
DR CPTAC; non-CPTAC-5574; -.
DR MaxQB; P70389; -.
DR PaxDb; P70389; -.
DR PeptideAtlas; P70389; -.
DR PRIDE; P70389; -.
DR ProteomicsDB; 296225; -.
DR DNASU; 16005; -.
DR GeneID; 16005; -.
DR KEGG; mmu:16005; -.
DR CTD; 3483; -.
DR MGI; MGI:107973; Igfals.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; P70389; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; P70389; -.
DR TreeFam; TF351124; -.
DR Reactome; R-MMU-4641263; Regulation of FZD by ubiquitination.
DR BioGRID-ORCS; 16005; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Igfals; mouse.
DR PRO; PR:P70389; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P70389; protein.
DR GO; GO:0042567; C:insulin-like growth factor ternary complex; ISS:BHF-UCL.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0005520; F:insulin-like growth factor binding; ISO:MGI.
DR GO; GO:0048495; F:Roundabout binding; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 19.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Glycoprotein; Leucine-rich repeat; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..603
FT /note="Insulin-like growth factor-binding protein complex
FT acid labile subunit"
FT /id="PRO_0000020696"
FT DOMAIN 32..74
FT /note="LRRNT"
FT REPEAT 75..96
FT /note="LRR 1"
FT REPEAT 99..120
FT /note="LRR 2"
FT REPEAT 123..144
FT /note="LRR 3"
FT REPEAT 147..168
FT /note="LRR 4"
FT REPEAT 171..192
FT /note="LRR 5"
FT REPEAT 195..216
FT /note="LRR 6"
FT REPEAT 219..240
FT /note="LRR 7"
FT REPEAT 243..264
FT /note="LRR 8"
FT REPEAT 267..288
FT /note="LRR 9"
FT REPEAT 291..312
FT /note="LRR 10"
FT REPEAT 315..336
FT /note="LRR 11"
FT REPEAT 339..360
FT /note="LRR 12"
FT REPEAT 363..384
FT /note="LRR 13"
FT REPEAT 387..408
FT /note="LRR 14"
FT REPEAT 411..432
FT /note="LRR 15"
FT REPEAT 435..456
FT /note="LRR 16"
FT REPEAT 459..480
FT /note="LRR 17"
FT REPEAT 483..504
FT /note="LRR 18"
FT REPEAT 507..528
FT /note="LRR 19"
FT DOMAIN 535..603
FT /note="LRRCT"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 71
FT /note="G -> S (in Ref. 2; BAB23677)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 603 AA; 66960 MW; 4A6223AEC7026BCC CRC64;
MALRTGSPAL VVLLAFWVAL GPCYLQGTDP GASADAEGPQ CPVTCTCSYD DYTDELSVFC
SSRNLTQLPD GIPVSTRALW LDGNNLSSIP SAAFQNLSSL DFLNLQGSWL RSLEPQALLG
LQNLYHLHLE RNLLRSLAAG LFRHTPSLAS LSLGNNLLGR LEEGLFRGLS HLWDLNLGWN
SLVVLPDTVF QGLGNLHELV LAGNKLTYLQ PALLCGLGEL RELDLSRNAL RSVKANVFIH
LPRLQKLYLD RNLITAVAPR AFLGMKALRW LDLSHNRVAG LLEDTFPGLL GLHVLRLAHN
AITSLRPRTF KDLHFLEELQ LGHNRIRQLG EKTFEGLGQL EVLTLNDNQI HEVKVGAFFG
LFNVAVMNLS GNCLRSLPEH VFQGLGRLHS LHLEHSCLGR IRLHTFAGLS GLRRLFLRDN
SISSIEEQSL AGLSELLELD LTANQLTHLP RQLFQGLGQL EYLLLSNNQL TMLSEDVLGP
LQRAFWLDLS HNRLETPAEG LFSSLGRLRY LNLRNNSLQT FVPQPGLERL WLDANPWDCS
CPLKALRDFA LQNPGVVPRF VQTVCEGDDC QPVYTYNNIT CAGPANVSGL DLRDISETLF
VHC
