ID H0UW89_CAVPO Unreviewed; 655 AA.
AC H0UW89;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=SPARC-like protein 1 {ECO:0000256|PIRNR:PIRNR002574};
GN Name=SPARCL1 {ECO:0000313|Ensembl:ENSCPOP00000001315.2};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000001315.2, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000001315.2}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000001315.2};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|PIRNR:PIRNR002574}.
CC -!- SIMILARITY: Belongs to the SPARC family.
CC {ECO:0000256|ARBA:ARBA00006404, ECO:0000256|PIRNR:PIRNR002574}.
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DR EMBL; AAKN02033404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003469421.1; XM_003469373.3.
DR AlphaFoldDB; H0UW89; -.
DR STRING; 10141.ENSCPOP00000001315; -.
DR Ensembl; ENSCPOT00000001474.3; ENSCPOP00000001315.2; ENSCPOG00000001455.4.
DR GeneID; 100734715; -.
DR KEGG; cpoc:100734715; -.
DR CTD; 8404; -.
DR VEuPathDB; HostDB:ENSCPOG00000001455; -.
DR eggNOG; KOG4004; Eukaryota.
DR GeneTree; ENSGT00510000046787; -.
DR HOGENOM; CLU_026297_0_1_1; -.
DR InParanoid; H0UW89; -.
DR OMA; CKRGHVC; -.
DR OrthoDB; 4695638at2759; -.
DR TreeFam; TF319356; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000001455; Expressed in hypothalamus and 13 other cell types or tissues.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-UniRule.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-UniRule.
DR GO; GO:0099560; P:synaptic membrane adhesion; IEA:Ensembl.
DR CDD; cd16236; EFh_SPARC_SPARCL1; 1.
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; IPR016359; SPARC-like_p1.
DR InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
DR PANTHER; PTHR13866; SPARC OSTEONECTIN; 1.
DR PANTHER; PTHR13866:SF16; SPARC-LIKE PROTEIN 1; 1.
DR Pfam; PF09289; FOLN; 1.
DR Pfam; PF00050; Kazal_1; 1.
DR Pfam; PF10591; SPARC_Ca_bdg; 1.
DR PIRSF; PIRSF002574; SPARC-like_p1; 1.
DR SMART; SM00274; FOLN; 1.
DR SMART; SM00280; KAZAL; 1.
DR SUPFAM; SSF47473; EF-hand; 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, ECO:0000256|PIRNR:PIRNR002574};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530,
KW ECO:0000256|PIRNR:PIRNR002574};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR002574};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR002574};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..655
FT /note="SPARC-like protein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003541133"
FT DOMAIN 446..502
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 613..648
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 30..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 655 AA; 73967 MW; 3CDB4907827B844E CRC64;
MKTVPFLLCL LGTAVAIPTN ARFLPDHSKS TAEPLVMPDN KEIPIVSADA ADNEKETTGS
KENHPNHKAE QSSTLRSEEG THELSAEQDK TQSHELGLKE QDGDDELSVN LEYSTTEGNL
EPQEDTGEPQ KKKLQEDTDF SASNVSSLVD SNQQENITKG EGYQEQPGND SHLQLDKNST
QSQDLREEES QEQDANIPNG KEEEETEPGK ADTPTDNPDK EKEFPEDNSN SKQEDNEQPD
DILEEANQPT QVSKMQEDEL EQGSQEKEED NSNVGLEEDS ASNISEHTPD TERQSQEGKM
GLKAIGDHKD IDKKTVSEAL LLDPTDVNHM TPRNHGADTD NDDSKHSAGD DYFVPSQDFT
EAEKAQSISY HLKYEEERDR AHKNENVDAS EPADHQEDKN AQSSSNEEEA SSEGHMRAHG
TDSCVNFQCK RGHVCKAEPQ GTPHCVCQDP ETCPPAKPLD QACGTDNQTY ASSCHLFATK
CRLEGTKKGH QLQLDYFGAC KSIPVCTDFE VAQFPLRMRD WLKNILMQLY EPNPKHAGYL
NEKQRTKVKK IYLDEKRLLA GDHPIELLLR DFKKNYHMYV YPVHWQFSEL DRHPMDRVLT
HSELAPLRAS LVPMEHCITR FFEECDPNKD KHITLKEWGH CFGIKEEDID ENLLF
//