ALS_RAT
ID ALS_RAT Reviewed; 603 AA.
AC P35859;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Insulin-like growth factor-binding protein complex acid labile subunit;
DE Short=ALS;
DE Flags: Precursor;
GN Name=Igfals; Synonyms=Als;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1384485; DOI=10.1016/0006-291x(92)92385-b;
RA Dai J., Baxter R.C.;
RT "Molecular cloning of the acid-labile subunit of the rat insulin-like
RT growth factor binding protein complex.";
RL Biochem. Biophys. Res. Commun. 188:304-309(1992).
RN [2]
RP PROTEIN SEQUENCE OF 24-44, AND CHARACTERIZATION.
RC STRAIN=Wistar; TISSUE=Serum;
RX PubMed=7507839; DOI=10.1210/endo.134.2.7507839;
RA Baxter R.C., Dai J.;
RT "Purification and characterization of the acid-labile subunit of rat serum
RT insulin-like growth factor binding protein complex.";
RL Endocrinology 134:848-852(1994).
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.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Brain, kidney, lung, heart, spleen, muscle and
CC liver.
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; S46785; AAB23770.2; -; mRNA.
DR PIR; JC1282; JC1282.
DR RefSeq; NP_445781.2; NM_053329.2.
DR AlphaFoldDB; P35859; -.
DR SMR; P35859; -.
DR STRING; 10116.ENSRNOP00000020233; -.
DR GlyGen; P35859; 7 sites.
DR PaxDb; P35859; -.
DR GeneID; 79438; -.
DR KEGG; rno:79438; -.
DR UCSC; RGD:68429; rat.
DR CTD; 3483; -.
DR RGD; 68429; Igfals.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; P35859; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; P35859; -.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR PRO; PR:P35859; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0042567; C:insulin-like growth factor ternary complex; IDA:RGD.
DR GO; GO:0005520; F:insulin-like growth factor binding; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEP:RGD.
DR GO; GO:0071378; P:cellular response to growth hormone stimulus; IEP:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
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; Direct protein sequencing; Glycoprotein;
KW Leucine-rich repeat; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:7507839"
FT CHAIN 24..603
FT /note="Insulin-like growth factor-binding protein complex
FT acid labile subunit"
FT /id="PRO_0000020698"
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"
SQ SEQUENCE 603 AA; 66812 MW; DCD7637D94A5037C CRC64;
MALRTGGPAL VVLLAFWVAL GPCHLQGTDP GASADAEGPQ CPVACTCSHD DYTDELSVFC
SSKNLTHLPD DIPVSTRALW LDGNNLSSIP SAAFQNLSSL DFLNLQGSWL RSLEPQALLG
LQNLYYLHLE RNRLRNLAVG LFTHTPSLAS LSLSSNLLGR LEEGLFQGLS HLWDLNLGWN
SLVVLPDTVF QGLGNLHELV LAGNKLTYLQ PALFCGLGEL RELDLSRNAL RSVKANVFVH
LPRLQKLYLD RNLITAVAPG AFLGMKALRW LDLSHNRVAG LMEDTFPGLL GLHVLRLAHN
AIASLRPRTF KDLHFLEELQ LGHNRIRQLG ERTFEGLGQL EVLTLNDNQI TEVRVGAFSG
LFNVAVMNLS GNCLRSLPER VFQGLDKLHS LHLEHSCLGH VRLHTFAGLS GLRRLFLRDN
SISSIEEQSL AGLSELLELD LTTNRLTHLP RQLFQGLGHL EYLLLSYNQL TTLSAEVLGP
LQRAFWLDIS HNHLETLAEG LFSSLGRVRY LSLRNNSLQT FSPQPGLERL WLDANPWDCS
CPLKALRDFA LQNPGVVPRF VQTVCEGDDC QPVYTYNNIT CAGPANVSGL DLRDVSETHF
VHC