ID A0A452I4S6_9SAUR Unreviewed; 1664 AA.
AC A0A452I4S6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000022564.1};
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:ENSGAGP00000022564.1, 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:ENSGAGP00000022564.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR Ensembl; ENSGAGT00000025707.1; ENSGAGP00000022564.1; ENSGAGG00000014979.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd22300; cc_LAMB1_C; 1.
DR CDD; cd00055; EGF_Lam; 13.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 9.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF233; LAMININ SUBUNIT BETA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; Laminin_EGF; 13.
DR Pfam; PF21199; LAMININ_IV_B; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 13.
DR PROSITE; PS01248; EGF_LAM_1; 4.
DR PROSITE; PS50027; EGF_LAM_2; 10.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020}.
FT DOMAIN 1..147
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 148..211
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 212..274
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 275..334
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 335..386
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 426..644
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 650..697
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 698..743
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 744..793
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 905..961
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 962..1009
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1010..1056
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT COILED 1231..1258
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1329..1391
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1439..1652
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 177..186
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 242..251
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 305..314
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 358..367
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 370..384
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 650..662
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 652..669
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 671..680
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 698..710
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 700..717
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 719..728
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 763..772
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 905..917
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 934..943
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 962..974
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 964..981
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 983..992
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1010..1022
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1012..1029
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1031..1040
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1664 AA; 184353 MW; 23AD0E4F567E4990 CRC64;
CVVAYINICC FLFLFFLKTF RPAAMLIERS SDFGKTWKVY RYFAYDCENS FPGISTGPMK
KVDDIICDSR YSDIEPSTEG EVIYRALDPA FRIEDPYSPR IQNLLKITNL RISFTKLHTL
GDNLLDSRME IKEKYYYAIY DMVVRGNCFC YGHASECAPV DGFNEEVEGM VHGHCMCRHN
TKGLNCELCL DFYHDLPWRP AEGRHSNACK KCNCNGHSIQ CHFDMAVYMA TGNTSGGVCD
DCQHNTMGHN CEQCKPFYFQ HPEREIRDPN ICEPCNCDPL GSQNGGICDR YTDFSAGLIA
GQCRCKLFVE GERCDLCKEG FYGLSADNPL GCQSCACNPL GTLPGGNPCD SETGSCYCKR
LATGRHCEQC LPEHWGLSND MDGCRPCDCD QGGAINNNCS SETGQCQCRP HMIGRQCNEV
ESGYYFMSLD HYIYEAEEAN FGPGVSIVER QYSQDRTPSW TGIGFVRVPE GAYLEFYVDN
IPYSMEYDVV IRYEPQLPDH WEKVVITVSR PGKIPTSSRC GNTVPDDDNQ TVSLSPGSRY
VVLPRPVCFE KGLNYTVRLE LSQYSSFDTE VESPYTLIDS LVLMPYCKSL DIFTVGGSGE
DVVTNSAWET FQRYRCLENS RSVVKTPMTD VCKNIIFSIS ALLHETALSC QCNPQGSLSS
VCDSNGGRCQ CRPNVVGRRC DRCAPGTFGF GPNGCKSCEC HLQGSVSSFC HPETGQCYCF
HGVYGRQCDR CLPGHWGFPS CQPCQCNGHT DDCDPYTGEC LNCRDSTTGH NCERCLGGYY
GDPVLGSGDH CRPCPCPDGP ESGRQFASSC YQDPITLQIV CVCNVGYIGS RCDECASGFF
GDPEERGGVC QPCQCNNNID MTDPGACDEQ SGKCLNCLYQ TEGENCQLCK YGYYGHALQQ
DCRKCVCNYL GTVREHCNSS EDCQCEKTTG QCQCLPNVTG QNCDRCAPNT WRLASGTGCE
LCECDVARSF RPSCNEFTGQ CQCMPGFGGR TCRECQEFFW GDPDVACQAC DCDPRGIQTP
QCNRSTGLCA CKEGVEGPHC DKCTRGYSGI FPDCVPCHQC FAVWDVIISE LTNRTQRFLE
RAKILKISGV SGPYQQTINT MEEKLNEIKS ILAQNPAAEP LKNIGNLFEE AGKLTADVTE
KMAEIEDKLS VIALKSNNTD THLRALETDA ESLDYVVKEL AEQLEFIKIS DIRGALDSIT
KYFQMSLEAE ERVNASTVHP DSLVELSAQT RQEVEDLISE QEAQFKAKQE EQSRLLDELA
GKLQSLDLSE VAEKTCGTPS GASCADSECG GLNCRTDEGE KKCGGPGCEG LVTVAHSAWQ
KAMDFDRDIL SALAEVEELS KMVSEAKQRA DKAKQNAQEV LLKTNATKEQ VDRSNEDLRN
LIKQIREFLM QDSADLDSIE AVANEVLKME MPSSPQQLQT LTEDIRERVE SLSDVEIILQ
QSAGDIARAE MLLEEANKAS KSAKDVKVTA AIVKEALEEA EKAQNAAGKA IKQAEEDIRG
TQDLLTSIES ENAASEETLN NATLRLTELE KSVEGLKQKA ATNSENVEEI EETIATVKQN
AEEVKEVLDS ELHAKYKTVE NLIAKKTEES ADARKKAGML QNEAKSLLAQ ANSKLQLLKD
LESTYENNQK VLEDKAKQLV ELEETVRSLL QAISQKVAVY STCL
//