ID A0A452GQP2_9SAUR Unreviewed; 3701 AA.
AC A0A452GQP2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000004012.1};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000004012.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000004012.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR Ensembl; ENSGAGT00000004674.1; ENSGAGP00000004012.1; ENSGAGG00000002525.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR GO; GO:0072359; P:circulatory system development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 3.
DR CDD; cd00055; EGF_Lam; 8.
DR CDD; cd00096; Ig; 4.
DR CDD; cd05754; IgI_Perlecan_like; 1.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 18.
DR Gene3D; 2.10.25.10; Laminin; 11.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR44170:SF30; FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF07679; I-set; 6.
DR Pfam; PF13927; Ig_3; 12.
DR Pfam; PF00052; Laminin_B; 3.
DR Pfam; PF00053; Laminin_EGF; 9.
DR Pfam; PF00054; Laminin_G_1; 3.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00180; EGF_Lam; 8.
DR SMART; SM00409; IG; 18.
DR SMART; SM00408; IGc2; 18.
DR SMART; SM00406; IGv; 5.
DR SMART; SM00281; LamB; 3.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 7.
DR SUPFAM; SSF48726; Immunoglobulin; 18.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01248; EGF_LAM_1; 7.
DR PROSITE; PS50027; EGF_LAM_2; 5.
DR PROSITE; PS50835; IG_LIKE; 18.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
DR PROSITE; PS51115; LAMININ_IVA; 3.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022869};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 59..244
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 278..327
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 462..639
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 673..722
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 784..833
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 961..1143
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1177..1226
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1227..1284
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1289..1377
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1383..1471
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1498..1581
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1588..1673
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1682..1764
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1775..1857
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1872..1954
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1968..2044
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2061..2143
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2158..2240
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2255..2337
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2351..2439
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2442..2530
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2541..2620
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2627..2709
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2719..2801
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2806..2890
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2895..2971
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2983..3159
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3155..3192
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3195..3233
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3239..3419
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3415..3452
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3454..3487
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3512..3699
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1322..1342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3335..3357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 297..306
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 692..701
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 784..796
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 804..813
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1196..1205
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1255..1264
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 3182..3191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3204..3221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3223..3232
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3442..3451
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3477..3486
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 3701 AA; 398046 MW; 99D47FF3B758EC3A CRC64;
MVFGIPDGVL SLTPRRGPCP EGYFHVEGTS KCLPCFCFGI TTACHGTSRY RDQIRLRFDT
PDDFKGVNVT TPAQPGTLPL SSTQLQIDPA LQEFQLVDLS RRFLTHDSFW TLPSQFLGNK
VDSYGGYLSF KVRYGLARGQ SEPVQKSNVV IVGNGQKLIY RVQVPTQPSV VNQRQIHFTE
ENWQQESGAP VSREMLLLAL QNLESILVQT VYDNKMASVG LSDIAMDTTT MELTSQGVAQ
GVEECRCPIG YSGLSCERCD ARFERVREGP YLGTCSGCNC HGHSSSCDRV YGYCLNCQHN
TEGPQCNKCK PGFFGDATRG NATACRPCPC PYTDPARRFS DTCFLDTDGQ ATCDACAQGY
TGRRCESCAR GYEGNPMQPG GSCVRTSQEI IQCDERGSSD STGGACRCKP NVAGRLCNEC
TSGAFHLSEQ NPDGCLKCFC MGVSQQCASS YWNREQVRAL DGERAHFSLA NLANTRTVSE
GIRSPGHAEL AFSAFNTLPR DVYYWVLPDR FKGDKVTSYG GELHYTITHS AAPGAQPLPG
QPDVRLRGNG IFLEHFAEAG PLPRTPTRFT VPFRERAWRR ADGQDATREH LLMALADIDL
FMIRASYMDR PAESRLSNIH MDVAVPHATG LERAVEVEEC TCPPGYRGPS CQDCDVGYAR
TSSGLYLGTC ERCDCSGHSG ECDAETGDCQ NCQDNTEGTR CERCQPGYYG DARQGTPTDC
QPCPCHGPYA TSQATKTCFL DMDGQPTCDA CTAGYVGRQC QRCAAGYVGN PSLGQPCREL
NRNCSCDPQG SVSRQCDARG QCQCKPHVEG PSCSSCRANH FHLSTENREG CLPCFCMGVT
QQCTSSSYYR GLVTSPFLPG DFQNFALVNR QHSTRIVTGF AVELSAEGPQ LSFGRFGQLG
QESYYWQLPE PYQGDKRETY FARMRRAHEN GTSLMEEQLR KAVASGRILG SGGGSHRARQ
VAKPQWEALL RPRFQESSNL LSQGHRLAAA AEKYSLVYKG FSLLPESVFY WQLPGAFLGD
KVGSYGGRLR YTLSYSSGGR SAPLPDADVQ ITGNDITLVA YQPELLPRDW RSFEIIFQEQ
YWKRPDGQHA TREHLMMALA DLDEILIRAT YSTDMVSASI AGISMETAMP TYSSLPLALE
VEECHCPPGY QGLSCQDCAA GYTRTGGGLY LGHCELCECN GHSDSCHPET GACSNCLHNA
AGEFCEQCAH GYYGDATTGT PEDCQPCACP LSEPENQFSR TCESLGGGGY RCSACEPGYT
GQYCEQCAPG YVGNPSVRGQ KCVPVDRAPF MVRVHPPKTT VSQGGEVTLR CQASGSPPYY
YSWSREDGRP VPSTAQSRRQ GEELHFPSIQ PSEAGVYVCT CRSLQHSNSS RAEVIVTEAP
SKPITVTVEE KRVQSVKPGA DVTFICTAKS KSPAYTLVWT RQNHGKLPRR AMDFNGILTI
RNVQPEDAGV YVCTGSNMLD MAEGMATLHV QAPPKTQMFY GPIEVMEGHR PSATAVLPTA
TIEPAQLTVQ PGQPAEFHCI ASGSPPPTVE WIGGQAGVMS RKAVIQGGTL RFPAVEPSDE
AEYLCRVRSS AGQHVARAFL QVHSASVPQV QVSPERTEVQ EGSTVRLYCR AAGSPTATIT
WEKQGGSLPP QSRSERTDIA TLVIPSITAA DSGVYLCIGT SPAGVGSARI EVVVLRASGV
VPPIRIEALS SSIAEGQTLD LKCLVTGQAP ATVTWYKRGG SLPARHQVSG SHLRISQVSA
ADSGEYVCRV SIGANSREAS IPVTVQHSAS SPHAPPIHIE SSSSAVTEGQ SLDLKCLVTG
QSPATVMWYK RGGSLPEGHQ VSGSHLRLVR VSVADSGEYV CRVSTSAGIQ ETSIIVTIYR
ATGSPYSSGI EPPVRIESSS SSISEGQTLD LQCLVTGQAP ATITWYKRGG SLPASHQVSG
SYLRIPQVLA ADAGEYVCRV STGTMVQEAS VIVTISSTGS SYSSGMRPPI WIEQSSSSVT
EGQTLDLKCL VTGQAPATVT WYKRGGSLPA DHQLSGSHLR LVQVSAADSG EYVCRAGTKE
ASVLVTIQQS SRISYPSGVT PPVRIESSSS SVAEGQTLDL NCLVAGQVQP RVTWHKRGGS
LPASHQVSGS RLRIPQVSAA DSGEYICHVN NGAGPLEASV IVTIPHSAGF LYPSGMAPPV
RIESSSSSIA EGQTLDLNCL VAGQAQPRVT WYKRGGSLPA SHQVSGSRLR IPQVSAADSG
EYVCRVSTGA VTQEAALVIT IEDSTSPSYS SGMAPPIRIE SSSSSITEGQ TLELQCLVAG
QAPAIVTWYK RGGSLPASHQ VSGSRLRLVQ VSAADSGEYV CRVSTSAGPR EASITVSVPS
GTSSSYRLQS PIISIEPHST AVRQGEDATF KCRIHGGARP INITWKMAPK QHLQDNVKIS
PNGSVITISR ARPSNQGAYR CVASNRYGVA NSVVNLMVQG SPTVSVMPKG PVTVKAGKSI
SLDCLGMGDP RPLVRWSRLG TRQKLEHQKL LPLESQAVLQ ILAAKPEDAG TYICMAQNSI
GSAQVQVEVS VEAANGKPGA PEITVKPTLT VVAGETATLQ CSATGDPPPS IQWSKLRAPL
PWQHRVVNNT LLIPRVAQQD SGQYICNASN AAGFTEAFVT LDVETPPYAT ILPEEVSVAA
GEAVRLQCLA HGTPPLRYQW SKTNGSLSSN AVLRESALHI SPTAPEDSGT YRCLVSNRVG
SAETFAQVSV QGSAPSASPT VRVTPQTVVK GVGGMAEFTC SVTGDARARI EWFREGGELP
TSHSVRNGVL RIQNLDRGCQ GVYTCRVSSP SGQAQDSARL VIQALPKVMI NMRTSVQSVL
VGAAVEFECL AIGDPKAHIT WSKVGSRIRP EVVISGGMVK IERVEQSDAG QYRCTATNDV
GTVQSNVILH VQSIPQIAAQ PEIREVTTGS RAVFPCLASG FPVPEIKWTK LEGDLPKDIC
LENNVLTIPS VKPEDAGIYV CTASNRQGKV TAFSMLKVRE RVVPYFTQNP RTFLALPTIK
DAYKKFEIQI TFRPDTADGM LLYNGQKKST GADFVSFGLV GGCPEFRFDA GSGMATIRHP
APIRLGEFHT VWLYRNLTQG SLVLDSHPPV NGTSQGKFQG LDLNEELYLG GYPDYIAIAK
SGLSSGFVGC VRQLLVQGEE VIFKDLDLKA HGVSNCPTCR DRPCQNGGVC RDSESSSYVC
HCPQEFTGSN CEHSQALHCH PEACGPDATC INRADGQGYR CRCHLGKSGE TCMEGIMATT
PSFNGSDSFI SYPPLTNIHY ELRLDTEFKP LSPDGLIMFS GGTGAPVEDF VSLSMASGHV
EFRYELGSGM AVLRSTEPLA LGQWHKVSAE RINKDGTLQV DSSKPVKRSS PGKSQGLNLR
TPMYLGGVDK SVTLPAAASI SSSFHGCIGE MSINGKKVDI SYSFLESRGV TQCYDSSPCD
RRPCLHGATC MPTGEYEFQC LCQDGFRGER CELSEDQCLL RNPCLNDGKC QANQCLCPAG
FSGTYCEQGP VPAALDREWA LEGSGGNDAP GQYGAYFQDG GYLALPRHVL PRSHPKSPET
IELEVRTRSL NGLLLWQGVE EGQNGKAKDF ISLGLRDGHL VFSYQLGSGE ANIVSEDPIN
DGEWHRVTAI REGRRGSIQV DGEELVSGES PGSNVMVNTQ GSVYIGGAPA IQALTAGKFR
SGITGCLKNL VLSSEPGQPP QQPIDLQHHS EAGVNMQECP S
//
