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Database: UniProt
Entry: A0A452I4S6_9SAUR
LinkDB: A0A452I4S6_9SAUR
Original site: A0A452I4S6_9SAUR 
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
//
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