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   24-JAN-2024, entry version 164.
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.ENSMUSP00000138695; -.
DR   GlyCosmos; P50405; 1 site, No reported glycans.
DR   GlyGen; P50405; 1 site.
DR   PhosphoSitePlus; P50405; -.
DR   CPTAC; non-CPTAC-3999; -.
DR   MaxQB; P50405; -.
DR   PaxDb; 10090-ENSMUSP00000066805; -.
DR   ProteomicsDB; 301867; -.
DR   Antibodypedia; 31946; 396 antibodies from 31 providers.
DR   DNASU; 20388; -.
DR   Ensembl; ENSMUST00000182014.10; ENSMUSP00000138204.4; ENSMUSG00000056370.18.
DR   GeneID; 20388; -.
DR   KEGG; mmu:20388; -.
DR   UCSC; uc057adr.1; mouse.
DR   AGR; MGI:109516; -.
DR   CTD; 6439; -.
DR   MGI; MGI:109516; Sftpb.
DR   eggNOG; KOG1340; Eukaryota.
DR   InParanoid; P50405; -.
DR   OMA; PKFWCQS; -.
DR   OrthoDB; 7299at2759; -.
DR   PhylomeDB; P50405; -.
DR   Reactome; R-MMU-5683826; Surfactant metabolism.
DR   BioGRID-ORCS; 20388; 2 hits in 58 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 cell types or 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   Gene3D; 1.10.225.10; Saposin-like; 2.
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   PANTHER; PTHR11480:SF33; PULMONARY SURFACTANT-ASSOCIATED PROTEIN B; 1.
DR   PANTHER; PTHR11480; SAPOSIN-RELATED; 1.
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; Saposin; 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
//