ID A0A3B3WZE8_9TELE Unreviewed; 930 AA.
AC A0A3B3WZE8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Thrombospondin 4a {ECO:0008006|Google:ProtNLM};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000008113.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000008113.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Sarcoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004369}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the thrombospondin family.
CC {ECO:0000256|ARBA:ARBA00009456}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A3B3WZE8; -.
DR Ensembl; ENSPMET00000003001.1; ENSPMEP00000008113.1; ENSPMEG00000009921.1.
DR Proteomes; UP000261480; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
DR Gene3D; 1.20.5.10; -; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 4.10.1080.10; TSP type-3 repeat; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR008859; Thrombospondin_C.
DR InterPro; IPR024665; TSP/COMP_coiled-coil.
DR InterPro; IPR046970; TSP/COMP_coiled-coil_sf.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR InterPro; IPR048287; TSPN-like_N.
DR PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR PANTHER; PTHR10199:SF92; THROMBOSPONDIN-4; 1.
DR Pfam; PF11598; COMP; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF02412; TSP_3; 6.
DR Pfam; PF05735; TSP_C; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF58006; Assembly domain of cartilage oligomeric matrix protein; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS51234; TSP3; 3.
DR PROSITE; PS51236; TSP_CTER; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00634}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Growth factor {ECO:0000256|ARBA:ARBA00023030};
KW Mitogen {ECO:0000256|ARBA:ARBA00023246};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sarcoplasmic reticulum {ECO:0000256|ARBA:ARBA00022951};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Unfolded protein response {ECO:0000256|ARBA:ARBA00023230}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..930
FT /note="Thrombospondin 4a"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017474061"
FT DOMAIN 293..330
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 466..501
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 525..560
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 662..697
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 701..915
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 463..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..486
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..642
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 930 AA; 102017 MW; E566AF7D0BEAE108 CRC64;
MIGAMALLIA EVAVYDLLTS PDCLPDLLQG GLAEQGVNEA FILTTFKLQP KTGTTLFGLF
NPRDNSKYFE FTVMGKLNRA VLRYLRTDKR MSSVSFNNLV LADGQQHRLL FHLKGLQQQG
PGGVELHLDC RLVETVRDLP AAFQGLPAGY GMVELKTMQA RDQESLDELK LVVGDSFENV
ASLQDCHFQQ RDSVQTLGVN TKQLSNQMLE LTKVINELKD VLIQQVKETS FLRNTISECQ
ACGLGGTEVV PEVKPRCAPG VCFRDDMCIE TANGVECAPC PDGYTGDGFN CDDVDECQFN
PCFPGVKCVN TAPGFRCDAC PLGYAGLPVE GVGILFAQTN KQVCDDIDEC KGPDNGGCTA
NSICHNSVGS FYCGSCKTGF TGDQVRGCEP ELSCGNSLTN PCDINAECIR ERDGSISCQC
GIGWAGNGYL CGKDTDIDGY PDEKLKCKDA NCRKDNCIFV PNSGQEDADR DGQGDACDDD
ADGDGIPNEQ DNCRLKPNVD QRNSDADSHG DACDNCRVVN NPDQRDTDGD GKGDACDDDM
DGDGVRNFLD NCQRVQNRDQ LDRDGDGVGD ACDSCPDIPN PNQSDVDNDL VGDSCDTNQD
SDGDGHQDTK DNCPLVINSS QLDTDKDGVG DECDDDDDND GIPDTLPPGP DNCRLVPNPD
QIDDNNDGVG DICESDFDQD KVIDRIDNCP ENAEVTLTDF RAYQTVVLDP EGDAQIDPNW
VVLNQGMEIV QTMNSDPGLA VGYTAFSGVD FEGTFHVNTV TDDDYAGFIF GYQDSSSFYV
VMWKQTEQTY WQATPFRAVA EPGIQLKAVK SRSGPGEHLR NSLWHTGDTN DQVRLLWKDP
RNVGWKDKVS YRWYLQHRPQ IGYIRVRFYE GTQLVADSGV TIDTTMRGGR LGVFCFSQEN
IIWSNLKYRC NDTIPEDFQE FSAQHTVDSI
//
