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Database: UniProt
Entry: A0A3Q0QWB5_AMPCI
LinkDB: A0A3Q0QWB5_AMPCI
Original site: A0A3Q0QWB5_AMPCI 
ID   A0A3Q0QWB5_AMPCI        Unreviewed;       637 AA.
AC   A0A3Q0QWB5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=SPARC-like 1 {ECO:0008006|Google:ProtNLM};
OS   Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC   Cichlasomatinae; Heroini; Amphilophus.
OX   NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000002487.1, ECO:0000313|Proteomes:UP000261340};
RN   [1] {ECO:0000313|Ensembl:ENSACIP00000002487.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the SPARC family.
CC       {ECO:0000256|ARBA:ARBA00006404}.
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DR   AlphaFoldDB; A0A3Q0QWB5; -.
DR   STRING; 61819.ENSACIP00000002487; -.
DR   Ensembl; ENSACIT00000002578.1; ENSACIP00000002487.1; ENSACIG00000002013.1.
DR   GeneTree; ENSGT00510000046787; -.
DR   OMA; GLHKTSH; -.
DR   Proteomes; UP000261340; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   Gene3D; 3.30.60.30; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR003645; Fol_N.
DR   InterPro; IPR015369; Follistatin/Osteonectin_EGF.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   InterPro; IPR001999; Osteonectin_CS.
DR   InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
DR   PANTHER; PTHR13866; SPARC OSTEONECTIN; 1.
DR   PANTHER; PTHR13866:SF25; SPARC-LIKE 1; 1.
DR   Pfam; PF09289; FOLN; 1.
DR   Pfam; PF00050; Kazal_1; 1.
DR   Pfam; PF10591; SPARC_Ca_bdg; 1.
DR   SMART; SM00274; FOLN; 1.
DR   SMART; SM00280; KAZAL; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
DR   PROSITE; PS00612; OSTEONECTIN_1; 1.
DR   PROSITE; PS00613; OSTEONECTIN_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..637
FT                   /note="SPARC-like 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018609477"
FT   DOMAIN          427..484
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          595..630
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          66..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..81
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..166
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..269
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..310
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   637 AA;  72028 MW;  F182A74C3B5B3B9A CRC64;
     MRACLVFLCL LAATFALSVS SKVIVIIKLT SKIFSKYFSS LLLKDAITEE ANKPKILPTL
     VTFEASSQEQ EDEELSSEDN ANKEDEEGAE KREKSTAVLL SEEELADLLK KEAEEDDEAE
     ARELEEEEVG ADKGKVESSE AVEITEDQKK NLDSNSEAKT DLPDEEEVKE ETVEDVVEEK
     VQKTTHSEKK KEPIGKMGDS EALPEEDGST ESVIPVDLDY AADSSLLQHL QTAPANVKTH
     SDDTKSVSKT DIPDVKEKET NEKELASIAD DYEQGMQNTE AAHSEELELR ARLSGKEEEK
     SKNDSGSHTK GKTRKQKKNQ RARKHSPHRD ETQPEQEQSQ QDPQESEGSN IDNTVQKAKR
     RRAGKWGPLV GMNPVQIRAT VDLYPMARPS LGGGIHLPET PADLCENFRC KRGKMCKLDA
     DNKPGCVCQE PSECPPSVNE FDHVCGTDNK TYDTSCELFA TKCNLEGTKK GHKLHLDYTG
     PCKLIPQCVD TELVQFPLRM RDWLKNVLLQ LYEHDSMTPG FLTPKQRFRV KKIFESERRL
     HAGDHSVELL AQDFEKNYNM YIYPVHWQFA QLDQHPSDRF LSHSELAPLR VPLVPMEHCT
     SRFFEECDAD KDKQVSFKEW ISCFGIKNED MDVNLLF
//
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