PSPB_MOUSE
ID PSPB_MOUSE Reviewed; 377 AA.
AC P50405;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Pulmonary surfactant-associated protein B;
DE Short=SP-B;
DE AltName: Full=Pulmonary surfactant-associated proteolipid SPL(Phe);
DE Flags: Precursor;
GN Name=Sftpb; Synonyms=Sftp3;
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=DBA/2J; TISSUE=Liver;
RX PubMed=7900819; DOI=10.1152/ajplung.1995.268.3.l381;
RA Bruno M.A., Bohinski R.J., Carter J.E., Foss K.A., Whitsett J.A.;
RT "Structure and function of the mouse surfactant protein B gene.";
RL Am. J. Physiol. 268:L381-L389(1995).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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: Pulmonary surfactant-associated proteins promote alveolar
CC stability by lowering the surface tension at the air-liquid interface
CC in the peripheral air spaces. SP-B increases the collapse pressure of
CC palmitic acid to nearly 70 millinewtons per meter.
CC -!- SUBUNIT: Homodimer; disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, surface film.
CC -!- MISCELLANEOUS: Pulmonary surfactant consists of 90% lipid and 10%
CC protein. There are 4 surfactant-associated proteins: 2 collagenous,
CC carbohydrate-binding glycoproteins (SP-A and SP-D) and 2 small
CC hydrophobic proteins (SP-B and SP-C).
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DR EMBL; S78114; AAB34846.2; -; Genomic_DNA.
DR RefSeq; NP_680088.1; NM_147779.2.
DR PDB; 6VYN; X-ray; 2.20 A; A/B/C/D/E/F/G/H=61-146.
DR PDB; 6VZ0; X-ray; 1.75 A; A/B=292-367.
DR PDB; 6VZD; X-ray; 1.88 A; A/B/C/E=61-146.
DR PDB; 6VZE; X-ray; 1.90 A; A/B/C/D/E/F/G/H=292-367.
DR PDB; 6W1B; X-ray; 2.31 A; A/B/C/D/E/F/G/H=61-146.
DR PDB; 7MBK; X-ray; 2.17 A; A/B=61-146.
DR PDBsum; 6VYN; -.
DR PDBsum; 6VZ0; -.
DR PDBsum; 6VZD; -.
DR PDBsum; 6VZE; -.
DR PDBsum; 6W1B; -.
DR PDBsum; 7MBK; -.
DR AlphaFoldDB; P50405; -.
DR SMR; P50405; -.
DR STRING; 10090.ENSMUSP00000066805; -.
DR GlyGen; P50405; 1 site.
DR PhosphoSitePlus; P50405; -.
DR CPTAC; non-CPTAC-3999; -.
DR MaxQB; P50405; -.
DR PaxDb; P50405; -.
DR PRIDE; P50405; -.
DR ProteomicsDB; 301867; -.
DR Antibodypedia; 31946; 361 antibodies from 31 providers.
DR DNASU; 20388; -.
DR Ensembl; ENSMUST00000182014; ENSMUSP00000138204; ENSMUSG00000056370.
DR GeneID; 20388; -.
DR KEGG; mmu:20388; -.
DR UCSC; uc057adr.1; mouse.
DR CTD; 6439; -.
DR MGI; MGI:109516; Sftpb.
DR eggNOG; KOG1340; Eukaryota.
DR InParanoid; P50405; -.
DR OMA; APHTICS; -.
DR OrthoDB; 865505at2759; -.
DR PhylomeDB; P50405; -.
DR Reactome; R-MMU-5683826; Surfactant metabolism.
DR BioGRID-ORCS; 20388; 2 hits in 55 CRISPR screens.
DR ChiTaRS; Sftpb; mouse.
DR PRO; PR:P50405; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P50405; protein.
DR Bgee; ENSMUSG00000056370; Expressed in lung and 25 other tissues.
DR ExpressionAtlas; P50405; baseline and differential.
DR GO; GO:0097208; C:alveolar lamellar body; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IEA:InterPro.
DR GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:UniProtKB-KW.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:InterPro.
DR InterPro; IPR003119; SAP_A.
DR InterPro; IPR007856; SapB_1.
DR InterPro; IPR008138; SapB_2.
DR InterPro; IPR008373; Saposin.
DR InterPro; IPR011001; Saposin-like.
DR InterPro; IPR008139; SaposinB_dom.
DR Pfam; PF02199; SapA; 1.
DR Pfam; PF05184; SapB_1; 1.
DR Pfam; PF03489; SapB_2; 2.
DR PRINTS; PR01797; SAPOSIN.
DR SMART; SM00162; SAPA; 1.
DR SMART; SM00741; SapB; 3.
DR SUPFAM; SSF47862; SSF47862; 3.
DR PROSITE; PS51110; SAP_A; 1.
DR PROSITE; PS50015; SAP_B; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Gaseous exchange; Glycoprotein;
KW Reference proteome; Repeat; Secreted; Signal; Surface film.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..191
FT /id="PRO_0000031650"
FT CHAIN 192..270
FT /note="Pulmonary surfactant-associated protein B"
FT /id="PRO_0000031651"
FT PROPEP 271..377
FT /id="PRO_0000031652"
FT DOMAIN 24..64
FT /note="Saposin A-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00414"
FT DOMAIN 64..146
FT /note="Saposin B-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 195..272
FT /note="Saposin B-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 291..366
FT /note="Saposin B-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 68..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 71..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 99..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 199..268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 202..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 226..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 239
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 295..362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 298..356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 321..331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT HELIX 67..81
FT /evidence="ECO:0007829|PDB:6VZD"
FT HELIX 85..99
FT /evidence="ECO:0007829|PDB:6VZD"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:6VZD"
FT HELIX 111..127
FT /evidence="ECO:0007829|PDB:6VZD"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:6VZD"
FT HELIX 293..324
FT /evidence="ECO:0007829|PDB:6VZ0"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:6VZ0"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:6VZ0"
FT HELIX 349..358
FT /evidence="ECO:0007829|PDB:6VZ0"
SQ SEQUENCE 377 AA; 41728 MW; CB687A82BA3FC56C CRC64;
MAKSHLLQWL LLLPTLCCPG AAITSASSLE CAQGPQFWCQ SLEHAVQCRA LGHCLQEVWG
HAGANDLCQE CEDIVHLLTK MTKEDAFQEA IRKFLEQECD ILPLKLLVPR CRQVLDVYLP
LVIDYFQSQI NPKAICNHVG LCPRGQAKPE QNPGMPDAVP NPLLDKLVLP VLPGALLARP
GPHTQDFSEQ QLPIPLPFCW LCRTLIKRVQ AVIPKGVLAV AVSQVCHVVP LVVGGICQCL
AERYTVLLLD ALLGRVVPQL VCGLVLRCST EDAMGPALPA VEPLIEEWPL QDTECHFCKS
VINQAWNTSE QAMPQAMHQA CLRFWLDRQK CEQFVEQHMP QLLALVPRSQ DAHITCQALG
VCEAPASPLQ CFQTPHL
