ID   SUSD4_PONAB             Reviewed;         489 AA.
AC   Q5R8M2;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Sushi domain-containing protein 4;
DE   Flags: Precursor;
GN   Name=SUSD4;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as complement inhibitor by disrupting the formation of
CC       the classical C3 convertase. Isoform 3 inhibits the classical
CC       complement pathway, while membrane-bound isoform 1 inhibits deposition
CC       of C3b via both the classical and alternative complement pathways.
CC       {ECO:0000250|UniProtKB:Q5VX71}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
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DR   EMBL; CR859729; CAH91888.1; -; mRNA.
DR   RefSeq; NP_001126094.1; NM_001132622.1.
DR   AlphaFoldDB; Q5R8M2; -.
DR   SMR; Q5R8M2; -.
DR   STRING; 9601.ENSPPYP00000000193; -.
DR   PRIDE; Q5R8M2; -.
DR   GeneID; 100173047; -.
DR   KEGG; pon:100173047; -.
DR   CTD; 55061; -.
DR   eggNOG; ENOG502QU1F; Eukaryota.
DR   InParanoid; Q5R8M2; -.
DR   OrthoDB; 560016at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030449; P:regulation of complement activation; IEA:InterPro.
DR   CDD; cd00033; CCP; 4.
DR   InterPro; IPR042985; SUSD4.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   PANTHER; PTHR47007; PTHR47007; 1.
DR   Pfam; PF00084; Sushi; 4.
DR   SMART; SM00032; CCP; 4.
DR   SUPFAM; SSF57535; SSF57535; 4.
DR   PROSITE; PS50923; SUSHI; 4.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Membrane; Reference proteome; Repeat; Signal;
KW   Sushi; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..489
FT                   /note="Sushi domain-containing protein 4"
FT                   /id="PRO_0000251977"
FT   TOPO_DOM        41..318
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        319..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        340..489
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          54..118
FT                   /note="Sushi 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          119..178
FT                   /note="Sushi 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          177..238
FT                   /note="Sushi 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          240..303
FT                   /note="Sushi 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..471
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        56..98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        84..116
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        121..164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        146..176
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        179..223
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        209..236
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        242..288
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        273..301
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   489 AA;  53698 MW;  5241CA0BFFE29990 CRC64;
     MYHGMNPSNG DGFLEQQQQQ QPQSPQRLLA VILWFQLALC FGPAQLTGGF DDLQACADPG
     IPENGFRTPS GGVFFEGSVA RFHCQDGFKL KGATKRLCLK HFNGTLGWIP SDSSICVQED
     CRIPQIEDAE IHNKTYRHGE KLIITCHEGF KIRYPDLHNM VSLCRDDGTW NNLPICQGCL
     RPLASSNGYV NISEFQTSFP VGTVIYYRCF PGFKLDGSAY LECLHNLIWS SSPPRCLALE
     VCPLPPMVSH GDFVCHPRPC ERYNHGTVVE FYCDPGYSLT SDYKYITCQY GEWFPSYQVY
     CIKSEQTWPS THETLLTTWK IVAFTATSVL LVLLLVILAR MFQTKFKAHF PPRGPPRSSS
     SDPDFVVVDG VPVMLPSYDE AVSGGLSALG PGYMASVGQG CPLPVDDQSP PAYPGSGDTD
     TGPGESETCD SVSGSPELLQ SLYSPPRCQE STHPASDNPD TIASTAEEVA STSPGVDIAD
     EIPLMEEDP