K1KB4_MOUSE
ID K1KB4_MOUSE Reviewed; 256 AA.
AC P00757;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Kallikrein 1-related peptidase-like b4;
DE AltName: Full=7S nerve growth factor alpha chain;
DE AltName: Full=Alpha-NGF;
DE Flags: Precursor;
GN Name=Klk1b4; Synonyms=Klk-4, Klk4, Ngfa;
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].
RX PubMed=3848399; DOI=10.1002/j.1460-2075.1985.tb02327.x;
RA Evans B.A., Richards R.I.;
RT "Genes for the alpha and gamma subunits of mouse nerve growth factor are
RT contiguous.";
RL EMBO J. 4:133-138(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6395888; DOI=10.1021/bi00320a015;
RA Isackson P.J., Ullrich A., Bradshaw R.A.;
RT "Mouse 7S nerve growth factor: complete sequence of a cDNA coding for the
RT alpha-subunit precursor and its relationship to serine proteases.";
RL Biochemistry 23:5997-6002(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary 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 [4]
RP PROTEIN SEQUENCE OF 18-47; 113-141 AND 162-178.
RX PubMed=6712944; DOI=10.1021/bi00301a032;
RA Ronne H., Anundi H., Rask L., Peterson P.A.;
RT "7S Nerve growth factor alpha and gamma subunits are closely related
RT proteins.";
RL Biochemistry 23:1229-1234(1984).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 7S COMPLEX.
RC STRAIN=Swiss Webster; TISSUE=Submandibular gland;
RX PubMed=9351801; DOI=10.1016/s0969-2126(97)00280-3;
RA Bax B., Blundell T.L., Murray-Rust J., McDonald N.Q.;
RT "Structure of mouse 7S NGF: a complex of nerve growth factor with four
RT binding proteins.";
RL Structure 5:1275-1285(1997).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions per 7S complex. The Zn(2+) ions are bound at
CC the alpha-gamma interfaces.;
CC -!- SUBUNIT: 7S nerve growth factor is composed of two alpha chains, a beta
CC dimer composed of identical chains, and two gamma chains.
CC -!- PTM: The presence of Gln-24 prevents cleavage of the activation
CC peptide, which remains attached at the amino end of the mature alpha
CC chain.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- CAUTION: Has no demonstrable enzymatic activity. This may be due to
CC several critical changes in its sequence, relative to those of related
CC proteases. {ECO:0000305}.
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DR EMBL; X01800; CAA25931.1; -; Genomic_DNA.
DR EMBL; X01801; CAA25932.1; -; Genomic_DNA.
DR EMBL; M11434; AAA39819.1; -; mRNA.
DR EMBL; BC034518; AAH34518.1; -; mRNA.
DR CCDS; CCDS21200.1; -.
DR PIR; B91005; NGMSA.
DR RefSeq; NP_035045.2; NM_010915.4.
DR PDB; 1SGF; X-ray; 3.15 A; A/X=17-256.
DR PDBsum; 1SGF; -.
DR AlphaFoldDB; P00757; -.
DR SMR; P00757; -.
DR STRING; 10090.ENSMUSP00000076576; -.
DR MEROPS; S01.931; -.
DR MaxQB; P00757; -.
DR PaxDb; P00757; -.
DR PeptideAtlas; P00757; -.
DR PRIDE; P00757; -.
DR ProteomicsDB; 269140; -.
DR DNASU; 18048; -.
DR Ensembl; ENSMUST00000077354; ENSMUSP00000076576; ENSMUSG00000066513.
DR GeneID; 18048; -.
DR KEGG; mmu:18048; -.
DR UCSC; uc009gom.2; mouse.
DR CTD; 18048; -.
DR MGI; MGI:97320; Klk1b4.
DR VEuPathDB; HostDB:ENSMUSG00000066513; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; P00757; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P00757; -.
DR TreeFam; TF331065; -.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR BioGRID-ORCS; 18048; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Klk1b4; mouse.
DR EvolutionaryTrace; P00757; -.
DR PRO; PR:P00757; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P00757; protein.
DR Bgee; ENSMUSG00000066513; Expressed in submandibular gland and 45 other tissues.
DR ExpressionAtlas; P00757; baseline and differential.
DR Genevisible; P00757; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0008236; F:serine-type peptidase activity; ISO:MGI.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IDA:MGI.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:MGI.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Growth factor;
KW Metal-binding; Reference proteome; Serine protease homolog; Signal; Zinc.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:6712944"
FT CHAIN 18..256
FT /note="Kallikrein 1-related peptidase-like b4"
FT /id="PRO_0000027972"
FT DOMAIN 18..253
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 18..24
FT /note="Activation peptide homolog"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT DISULFID 45..61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 147..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 179..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 204..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VARIANT 184
FT /note="E -> K"
FT CONFLICT 44
FT /note="Q -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="E -> C (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:1SGF"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:1SGF"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:1SGF"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:1SGF"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:1SGF"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:1SGF"
FT HELIX 245..253
FT /evidence="ECO:0007829|PDB:1SGF"
SQ SEQUENCE 256 AA; 28548 MW; 9F6690E21982C3DC CRC64;
MWFLILFLAL SLGGIDAAPP VQSQVDCENS QPWHVAVYRF NKYQCGGVLL DRNWVLTAAH
CYNDKYQVWL GKNNFLEDEP SDQHRLVSKA IPHPDFNMSL LNEHTPQPED DYSNDLMLLR
LSKPADITDV VKPITLPTEE PKLGSTCLAS GWGSTTPIKF KYPDDLQCVN LKLLPNEDCD
KAHEMKVTDA MLCAGEMDGG SYTCEHDSGG PLICDGILQG ITSWGPEPCG EPTEPSVYTK
LIKFSSWIRE TMANNP
