PSPB_RAT
ID PSPB_RAT Reviewed; 376 AA.
AC P22355;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 135.
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 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].
RX PubMed=2920185; DOI=10.1016/0167-4838(89)90296-3;
RA Emrie P.A., Shannon J.M., Mason R.J., Fisher J.H.;
RT "cDNA and deduced amino acid sequence for the rat hydrophobic pulmonary
RT surfactant-associated protein, SP-B.";
RL Biochim. Biophys. Acta 994:215-221(1989).
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; X14778; CAA32885.1; -; mRNA.
DR PIR; S02766; S02766.
DR RefSeq; NP_620197.1; NM_138842.1.
DR AlphaFoldDB; P22355; -.
DR SMR; P22355; -.
DR STRING; 10116.ENSRNOP00000014505; -.
DR GlyGen; P22355; 1 site.
DR PaxDb; P22355; -.
DR GeneID; 192155; -.
DR KEGG; rno:192155; -.
DR UCSC; RGD:621700; rat.
DR CTD; 6439; -.
DR RGD; 621700; Sftpb.
DR eggNOG; KOG1340; Eukaryota.
DR InParanoid; P22355; -.
DR OrthoDB; 865505at2759; -.
DR PhylomeDB; P22355; -.
DR Reactome; R-RNO-5683826; Surfactant metabolism.
DR PRO; PR:P22355; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0097208; C:alveolar lamellar body; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005764; C:lysosome; IEA:InterPro.
DR GO; GO:0005771; C:multivesicular body; IDA:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0071732; P:cellular response to nitric oxide; IEP:RGD.
DR GO; GO:0007623; P:circadian rhythm; IEP:RGD.
DR GO; GO:0050828; P:regulation of liquid surface tension; TAS:RGD.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:UniProtKB-KW.
DR GO; GO:0070849; P:response to epidermal growth factor; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0070848; P:response to growth factor; IEP:RGD.
DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0070741; P:response to interleukin-6; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0033189; P:response to vitamin A; IEP:RGD.
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 2: Evidence at transcript level;
KW Disulfide bond; Gaseous exchange; Glycoprotein; Reference proteome; Repeat;
KW Secreted; Signal; Surface film.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..190
FT /id="PRO_0000031656"
FT CHAIN 191..269
FT /note="Pulmonary surfactant-associated protein B"
FT /id="PRO_0000031657"
FT PROPEP 270..376
FT /id="PRO_0000031658"
FT DOMAIN 25..63
FT /note="Saposin A-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00414"
FT DOMAIN 63..145
FT /note="Saposin B-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 194..271
FT /note="Saposin B-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 290..365
FT /note="Saposin B-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 67..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 70..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 98..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 198..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 201..261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 225..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 238
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 294..361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 297..355
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 320..330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
SQ SEQUENCE 376 AA; 41590 MW; F329DC62E733FB4C CRC64;
MAKLHLQWLL LLPTLCSLGA ATESASSPDC AQGPKFWCQS LEQAIQCRAL GHCLQEVWGH
AGANDLCQEC EDIVHLLTKM TKEDAFQDTI RKFLEQECDI LPLKLLVPRC RQVLDVYLPL
VIDYFQGQIK PKAICSHVGL CPLGQTKPEQ KPEMLDAIPN PLLNKLVLPA LPGAFLARPG
PHTQDLSEQQ LPIPLPFCWL CRTLIKRVQA VIPKGVLAVA VSQVCHVVPL VVGGICQCLA
ERYTVLLLDA LLGRVVPQLV CGLVLRCSTA DAIGPALPAL EPLIEKWPLQ DTECHFCKSV
INQAWNTSEQ AMPQAMHQAC LRFWLDRQKC EQFVEQHMPQ LLALVPRSQD AHTSCQALGV
CEAPASPLQC FQTPHL