PSPB_BOVIN
ID PSPB_BOVIN Reviewed; 373 AA.
AC P15781; Q148E8;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Pulmonary surfactant-associated protein B;
DE Short=SP-B;
DE AltName: Full=6 kDa protein;
DE AltName: Full=Pulmonary surfactant-associated proteolipid SPL(Phe);
DE Flags: Precursor;
GN Name=SFTPB; Synonyms=SFTP3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal lung;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 188-266.
RX PubMed=3689402; DOI=10.1016/s0006-291x(87)80288-7;
RA Olafson R.W., Rink U., Kielland S., Yu S.-H., Chung J., Harding P.G.R.,
RA Possmayer F.;
RT "Protein sequence analysis studies on the low molecular weight hydrophobic
RT proteins associated with bovine pulmonary surfactant.";
RL Biochem. Biophys. Res. Commun. 148:1406-1411(1987).
RN [3]
RP PROTEIN SEQUENCE OF 188-266, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18088070; DOI=10.1002/rcm.3345;
RA Liu S., Zhao L., Manzanares D., Doherty-Kirby A., Zhang C., Possmayer F.,
RA Lajoie G.A.;
RT "Characterization of bovine surfactant proteins B and C by electrospray
RT ionization mass spectrometry.";
RL Rapid Commun. Mass Spectrom. 22:197-203(2008).
RN [4]
RP PROTEIN SEQUENCE OF 188-197.
RX PubMed=3663690; DOI=10.1016/0005-2760(87)90070-1;
RA Yu S.-H., Chung W., Olafson R.W., Harding P.G.R., Possmayer F.;
RT "Characterization of the small hydrophobic proteins associated with
RT pulmonary surfactant.";
RL Biochim. Biophys. Acta 921:437-448(1987).
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; BC118395; AAI18396.1; -; mRNA.
DR PIR; A29667; A29667.
DR RefSeq; NP_001068779.1; NM_001075311.2.
DR RefSeq; XP_005212817.1; XM_005212760.2.
DR AlphaFoldDB; P15781; -.
DR SMR; P15781; -.
DR STRING; 9913.ENSBTAP00000042549; -.
DR PaxDb; P15781; -.
DR Ensembl; ENSBTAT00000045134; ENSBTAP00000042549; ENSBTAG00000021230.
DR GeneID; 507398; -.
DR KEGG; bta:507398; -.
DR CTD; 6439; -.
DR VEuPathDB; HostDB:ENSBTAG00000021230; -.
DR VGNC; VGNC:34528; SFTPB.
DR eggNOG; KOG1340; Eukaryota.
DR GeneTree; ENSGT00940000161711; -.
DR HOGENOM; CLU_063244_0_0_1; -.
DR InParanoid; P15781; -.
DR OMA; APHTICS; -.
DR OrthoDB; 865505at2759; -.
DR TreeFam; TF316942; -.
DR Reactome; R-BTA-5683826; Surfactant metabolism.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000021230; Expressed in lung and 10 other tissues.
DR GO; GO:0097208; C:alveolar lamellar body; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:InterPro.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
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; 2.
DR PROSITE; PS51110; SAP_A; 1.
DR PROSITE; PS50015; SAP_B; 3.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Gaseous exchange; Glycoprotein;
KW Reference proteome; Repeat; Secreted; Signal; Surface film.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..187
FT /id="PRO_0000285124"
FT CHAIN 188..266
FT /note="Pulmonary surfactant-associated protein B"
FT /id="PRO_0000175240"
FT PROPEP 267..373
FT /id="PRO_0000285125"
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 191..268
FT /note="Saposin B-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 287..362
FT /note="Saposin B-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 303
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 195..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 198..258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 222..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 235
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 291..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 294..352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 317..327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CONFLICT 198
FT /note="C -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="R -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 233..239
FT /note="CQCLVER -> IQQLVIE (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="L -> LT (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="Q -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="V -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="S -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 41060 MW; A41A31AE5A5C0F82 CRC64;
MAKSHLLPWL LLLPILCGPG TAAAITYSLA CAQGPEFWCQ SLEQALQCRA LGHCLQEVWG
HVEADDLCQE CENISRLLTK MAKEAIFQDS VRKFLEQECD VLPLKLLAPL CRHLLDTYFP
LIIEHFQSHM NPKFICQHVG LCKPRHPEPG KGPEPWGPLL DKLALPLLPG VPQAKPGPQT
QDLSEQLFPI PIPYCWLCRT LIKRIQAVIP KGVLAMTVAQ VCHVVPLLVG GICQCLVERY
SVILLDTLLG RMLPQLVCGL VLRCSSEDSA GPALPALGSV PGEWLPQDSD CQLCMFVTTQ
AGNSSEQATP QAMRQACLGT WLDRQKCERF VEENAPRLQT LVSSGWDAHM ACQALGTCAA
PFSPLQCVHS PHF
