PSPC_PIG
ID PSPC_PIG Reviewed; 35 AA.
AC P15785;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Pulmonary surfactant-associated protein C;
DE Short=SP-C;
DE AltName: Full=Pulmonary surfactant-associated proteolipid SPL(Val);
GN Name=SFTPC; Synonyms=SFTP2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3408709; DOI=10.1021/bi00410a002;
RA Johansson J., Curstedt T., Robertson B., Joernvall H.;
RT "Size and structure of the hydrophobic low molecular weight surfactant-
RT associated polypeptide.";
RL Biochemistry 27:3544-3547(1988).
RN [2]
RP PALMITOYLATION AT CYS-5 AND CYS-6.
RX PubMed=2326260; DOI=10.1073/pnas.87.8.2985;
RA Curstedt T., Johansson J., Persson P., Eklund A., Robertson B.,
RA Loewenadler B., Joernvall H.;
RT "Hydrophobic surfactant-associated polypeptides: SP-C is a lipopeptide with
RT two palmitoylated cysteine residues, whereas SP-B lacks covalently linked
RT fatty acyl groups.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2985-2989(1990).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=8180229; DOI=10.1021/bi00185a042;
RA Johansson J., Szyperski T., Curstedt T., Wuethrich K.;
RT "The NMR structure of the pulmonary surfactant-associated polypeptide SP-C
RT in an apolar solvent contains a valyl-rich alpha-helix.";
RL Biochemistry 33:6015-6023(1994).
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.
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 PIR; A28640; LNPGC1.
DR PDB; 1SPF; NMR; -; A=1-35.
DR PDB; 5NDA; NMR; -; A=3-35.
DR PDBsum; 1SPF; -.
DR PDBsum; 5NDA; -.
DR AlphaFoldDB; P15785; -.
DR BMRB; P15785; -.
DR SMR; P15785; -.
DR STRING; 9823.ENSSSCP00000010269; -.
DR SwissPalm; P15785; -.
DR PaxDb; P15785; -.
DR eggNOG; ENOG502S6QH; Eukaryota.
DR HOGENOM; CLU_087015_0_0_1; -.
DR EvolutionaryTrace; P15785; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P15785; SS.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:UniProtKB-KW.
DR InterPro; IPR018051; SP-C_palmitoylation_site.
DR InterPro; IPR015091; Surfactant_protein_propep.
DR Pfam; PF08999; SP_C-Propep; 1.
DR PROSITE; PS00341; SURFACT_PALMITOYL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Gaseous exchange; Lipoprotein;
KW Palmitate; Reference proteome; Secreted; Surface film.
FT CHAIN 1..35
FT /note="Pulmonary surfactant-associated protein C"
FT /id="PRO_0000183015"
FT LIPID 5
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:2326260"
FT LIPID 6
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:2326260"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:1SPF"
FT HELIX 9..33
FT /evidence="ECO:0007829|PDB:1SPF"
SQ SEQUENCE 35 AA; 3710 MW; C8A713AFF926F0FE CRC64;
LRIPCCPVNL KRLLVVVVVV VLVVVVIVGA LLMGL