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Database: UniProt
Entry: P50405
LinkDB: P50405
Original site: P50405 
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   29-OCT-2014, entry version 112.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DBA/2J; TISSUE=Liver;
RX   PubMed=7900819;
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).
CC   -!- FUNCTION: Pulmonary surfactant-associated proteins promote
CC       alveolar stability by lowering the surface tension at the air-
CC       liquid interface in the peripheral air spaces. SP-B increases the
CC       collapse pressure of palmitic acid to nearly 70 millinewtons per
CC       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
CC       collagenous, carbohydrate-binding glycoproteins (SP-A and SP-D)
CC       and 2 small hydrophobic proteins (SP-B and SP-C).
CC   -!- SIMILARITY: Contains 1 saposin A-type domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00414}.
CC   -!- SIMILARITY: Contains 3 saposin B-type domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00415}.
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DR   EMBL; S78114; AAB34846.2; -; Genomic_DNA.
DR   RefSeq; NP_680088.1; NM_147779.2.
DR   UniGene; Mm.46033; -.
DR   ProteinModelPortal; P50405; -.
DR   SMR; P50405; 68-142.
DR   IntAct; P50405; 1.
DR   MINT; MINT-4109008; -.
DR   STRING; 10090.ENSMUSP00000066805; -.
DR   MaxQB; P50405; -.
DR   PaxDb; P50405; -.
DR   PRIDE; P50405; -.
DR   GeneID; 20388; -.
DR   UCSC; uc009cid.1; mouse.
DR   CTD; 6439; -.
DR   MGI; MGI:109516; Sftpb.
DR   eggNOG; NOG286450; -.
DR   HOGENOM; HOG000115745; -.
DR   HOVERGEN; HBG006905; -.
DR   InParanoid; P50405; -.
DR   PhylomeDB; P50405; -.
DR   NextBio; 298318; -.
DR   PRO; PR:P50405; -.
DR   Bgee; P50405; -.
DR   CleanEx; MM_SFTPB; -.
DR   ExpressionAtlas; P50405; baseline and differential.
DR   Genevestigator; P50405; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005764; C:lysosome; IEA:InterPro.
DR   GO; GO:0007585; P:respiratory gaseous exchange; IEA:UniProtKB-KW.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.225.10; -; 3.
DR   InterPro; IPR003119; SapA.
DR   InterPro; IPR007856; SapB_1.
DR   InterPro; IPR008138; SapB_2.
DR   InterPro; IPR008373; Saposin.
DR   InterPro; IPR011001; Saposin-like.
DR   InterPro; IPR008139; SaposinB.
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   2: Evidence at transcript level;
KW   Complete proteome; Disulfide bond; Gaseous exchange; Glycoprotein;
KW   Reference proteome; Repeat; Secreted; Signal; Surface film.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   PROPEP       23    191
FT                                /FTId=PRO_0000031650.
FT   CHAIN       192    270       Pulmonary surfactant-associated protein
FT                                B.
FT                                /FTId=PRO_0000031651.
FT   PROPEP      271    377
FT                                /FTId=PRO_0000031652.
FT   DOMAIN       24     64       Saposin A-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00414}.
FT   DOMAIN       64    146       Saposin B-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00415}.
FT   DOMAIN      195    272       Saposin B-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00415}.
FT   DOMAIN      291    366       Saposin B-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00415}.
FT   CARBOHYD    307    307       N-linked (GlcNAc...).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00415}.
FT   DISULFID     68    142       {ECO:0000255|PROSITE-ProRule:PRU00415}.
FT   DISULFID     71    136       {ECO:0000255|PROSITE-ProRule:PRU00415}.
FT   DISULFID     99    111       {ECO:0000255|PROSITE-ProRule:PRU00415}.
FT   DISULFID    199    268       {ECO:0000255|PROSITE-ProRule:PRU00415}.
FT   DISULFID    202    262       {ECO:0000255|PROSITE-ProRule:PRU00415}.
FT   DISULFID    226    237       {ECO:0000255|PROSITE-ProRule:PRU00415}.
FT   DISULFID    239    239       Interchain. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00415}.
FT   DISULFID    295    362       {ECO:0000255|PROSITE-ProRule:PRU00415}.
FT   DISULFID    298    356       {ECO:0000255|PROSITE-ProRule:PRU00415}.
FT   DISULFID    321    331       {ECO:0000255|PROSITE-ProRule:PRU00415}.
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
//
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