CRUM1_HUMAN » Protein crumbs homolog 1

CRUM1_HUMAN » Protein crumbs homolog 1
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
CRUM1_HUMAN » Protein crumbs homolog 1 »
Hydrophobic Thickness 34.4 ± 2.6 Å
Tilt Angle 28 ± 0°
ΔGtransfer -29.5 kcal/mol
ΔGfold -25.5 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC
Topology Out
TM Segments 1343-1368 (1343-1374)
Pathways

Hippo signaling pathway (KEGG)

PDB 4uu5 (B=1390-1406)
OPM none
Complexes none
Interactions

EXT2, Complex: EXT2:CRUM1, PubMed

Domains

AA: 74-105, PDBID: 1TOZ, Subunit A, Seq Identity:51%, EGF-like domain

AA: 119-140, PDBID: 2YGQ, Subunit A, Seq Identity:41%, Human growth factor-like EGF

AA: 152-182, PDBID: 4XBM, Subunit B, Seq Identity:60%, EGF-like domain

AA: 190-220, PDBID: 1TOZ, Subunit A, Seq Identity:58%, EGF-like domain

AA: 233-254, PDBID: 2YGQ, Subunit A, Seq Identity:47%, Human growth factor-like EGF

AA: 266-297, PDBID: 1TOZ, Subunit A, Seq Identity:58%, EGF-like domain

AA: 305-335, PDBID: 1TOZ, Subunit A, Seq Identity:47%, EGF-like domain

AA: 343-393, PDBID: 4D90, Subunit B, Seq Identity:32%, EGF-like domain

AA: 401-434, PDBID: 3POY, Subunit A, Seq Identity:38%, EGF-like domain

AA: 445-479, PDBID: 3H5C, Subunit B, Seq Identity:44%, EGF-like domain

AA: 514-651, PDBID: 3B3Q, Subunit E, Seq Identity:17%, Laminin G domain

AA: 676-706, PDBID: 1EDM, Subunit B, Seq Identity:48%, EGF-like domain

AA: 743-860, PDBID: 3SH4, Subunit A, Seq Identity:21%, Laminin G domain

AA: 891-920, PDBID: 4XBM, Subunit B, Seq Identity:47%, EGF-like domain

AA: 980-1105, PDBID: 3SH4, Subunit A, Seq Identity:19%, Laminin G domain

AA: 1143-1173, PDBID: 1EDM, Subunit B, Seq Identity:60%, EGF-like domain

AA: 1181-1210, PDBID: 1TOZ, Subunit A, Seq Identity:50%, EGF-like domain

AA: 1223-1240, PDBID: 4D90, Subunit A, Seq Identity:52%, Human growth factor-like EGF

AA: 1301-1331, PDBID: 1BF9, Subunit A, Seq Identity:52%, EGF-like domain

UniProt annotation for CRUM1_HUMAN » Protein crumbs homolog 1
FUNCTION: Plays a role in photoreceptor morphogenesis in the retina. May maintain cell polarization and adhesion.

SUBUNIT: Forms a complex with MPDZ (By similarity). Forms a complex with MPP4 and MPP5.

TISSUE SPECIFICITY: Preferential expression in retina, also expressed in brain, testis, fetal brain and fetal eye.

DISEASE: Note=CRB1 mutations have been found in various retinal dystrophies, chronic and disabling disorders of visual function. They predominantly involve the posterior portion of the ocular fundus, due to degeneration in the sensory layer of the retina, retinal pigment epithelium, Bruch membrane, choroid, or a combination of these tissues. Onset of inherited retinal dystrophies is painless, bilateral and typically progressive. Most people experience gradual peripheral vision loss or tunnel vision, and difficulties with poor illumination and night vision. Central vision is usually unaffected, so the person may still be able to read. However, it can also deteriorate to cause total blindness. Examples of retinal dystrophies are retinitis pigmentosa, Leber congenital amaurosis, cone-rod dystrophy among others.

DISEASE: Retinitis pigmentosa 12 (RP12) OMIM: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. RP12 is an autosomal recessive, severe form often manifesting in early childhood. Patients experiment progressive visual field loss with severe visual impairment before the age of twenty. Some patients have a preserved paraarteriolar retinal pigment epithelium (PPRPE) and hypermetropia. Note=The disease is caused by mutations affecting the gene represented in this entry.

DISEASE: Leber congenital amaurosis 8 (LCA8) OMIM: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. mutations affecting the gene represented in this entry.

DISEASE: Pigmented paravenous chorioretinal atrophy (PPCRA) OMIM: Unusual retinal degeneration characterized by accumulation of pigmentation along retinal veins. PPCRA is dominantly inherited, but exhibited variable expressivity. Males are more likely to exhibit a severe phenotype, whereas females may remain virtually asymptomatic even in later years. The PPCRA phenotype is associated with a mutation in CRB1 gene which is likely to affect the structure of the CRB1 protein. mutations affecting the gene represented in this entry.

UniProt features for CRUM1_HUMAN » Protein crumbs homolog 1
SIGNAL 1 25 Potential.
CHAIN 26 1406 Protein crumbs homolog 1.
DOMAIN 30 68 EGF-like 1.
DOMAIN 70 108 EGF-like 2.
DOMAIN 110 146 EGF-like 3.
DOMAIN 148 184 EGF-like 4; calcium-binding (Potential).
DOMAIN 186 222 EGF-like 5; calcium-binding (Potential).
DOMAIN 224 260 EGF-like 6; calcium-binding (Potential).
DOMAIN 262 299 EGF-like 7; calcium-binding (Potential).
DOMAIN 301 337 EGF-like 8.
DOMAIN 339 395 EGF-like 9.
DOMAIN 397 439 EGF-like 10; calcium-binding (Potential).
DOMAIN 441 481 EGF-like 11.
DOMAIN 485 670 Laminin G-like 1.
DOMAIN 672 708 EGF-like 12.
DOMAIN 714 885 Laminin G-like 2.
DOMAIN 887 923 EGF-like 13.
DOMAIN 924 960 EGF-like 14.
DOMAIN 950 1137 Laminin G-like 3.
DOMAIN 1139 1175 EGF-like 15.
DOMAIN 1177 1212 EGF-like 16; calcium-binding (Potential).
DOMAIN 1214 1250 EGF-like 17.
DOMAIN 1255 1295 EGF-like 18.
DOMAIN 1297 1333 EGF-like 19; calcium-binding (Potential).
DISULFID 34 45 By similarity.
DISULFID 39 54 By similarity.
DISULFID 56 67 By similarity.
DISULFID 74 85 By similarity.
DISULFID 79 96 By similarity.
DISULFID 98 107 By similarity.
DISULFID 114 125 By similarity.
DISULFID 119 134 By similarity.
DISULFID 136 145 By similarity.
DISULFID 152 163 By similarity.
DISULFID 157 172 By similarity.
DISULFID 174 183 By similarity.
DISULFID 190 201 By similarity.
DISULFID 195 210 By similarity.
DISULFID 212 221 By similarity.
DISULFID 228 239 By similarity.
DISULFID 233 248 By similarity.
DISULFID 250 259 By similarity.
DISULFID 266 277 By similarity.
DISULFID 271 286 By similarity.
DISULFID 288 298 By similarity.
DISULFID 305 316 By similarity.
DISULFID 310 325 By similarity.
DISULFID 327 336 By similarity.
DISULFID 343 354 By similarity.
DISULFID 348 383 By similarity.
DISULFID 385 394 By similarity.
DISULFID 401 412 By similarity.
DISULFID 406 421 By similarity.
DISULFID 423 438 By similarity.
DISULFID 445 456 By similarity.
DISULFID 450 469 By similarity.
DISULFID 471 480 By similarity.
DISULFID 642 670 By similarity.
DISULFID 676 687 By similarity.
DISULFID 681 696 By similarity.
DISULFID 698 707 By similarity.
DISULFID 851 885 By similarity.
DISULFID 891 902 By similarity.
DISULFID 896 911 By similarity.
DISULFID 913 922 By similarity.
DISULFID 928 939 By similarity.
DISULFID 933 948 By similarity.
DISULFID 1096 1137 By similarity.
DISULFID 1143 1154 By similarity.
DISULFID 1148 1163 By similarity.
DISULFID 1165 1174 By similarity.
DISULFID 1181 1191 By similarity.
DISULFID 1186 1200 By similarity.
DISULFID 1202 1211 By similarity.
DISULFID 1218 1229 By similarity.
DISULFID 1223 1238 By similarity.
DISULFID 1240 1249 By similarity.
DISULFID 1259 1274 By similarity.
DISULFID 1268 1283 By similarity.
DISULFID 1285 1294 By similarity.
DISULFID 1301 1312 By similarity.
DISULFID 1306 1321 By similarity.
DISULFID 1323 1332 By similarity.
Amino Acid Sequence for CRUM1_HUMAN » Protein crumbs homolog 1
MALKNINYLL IFYLSFSLLI YIKNSFCNKN NTRCLSNSCQ NNSTCKDFSK DNDCSCSDTA NNLDKDCDNM KDPCFSNPCQ GSATCVNTPG ERSFLCKCPP GYSGTICETT IGSCGKNSCQ HGGICHQDPI YPVCICPAGY AGRFCEIDHD ECASSPCQNG AVCQDGIDGY SCFCVPGYQG RHCDLEVDEC ASDPCKNEAT CLNEIGRYTC ICPHNYSGVN CELEIDECWS QPCLNGATCQ DALGAYFCDC APGFLGDHCE LNTDECASQP CLHGGLCVDG ENRYSCNCTG SGFTGTHCET LMPLCWSKPC HNNATCEDSV DNYTCHCWPG YTGAQCEIDL NECNSNPCQS NGECVELSSE KQYGRITGLP SSFSYHEASG YVCICQPGFT GIHCEEDVNE CSSNPCQNGG TCENLPGNYT CHCPFDNLSR TFYGGRDCSD ILLGCTHQQC LNNGTCIPHF QDGQHGFSCL CPSGYTGSLC EIATTLSFEG DGFLWVKSGS VTTKGSVCNI ALRFQTVQPM ALLLFRSNRD VFVKLELLSG YIHLSIQVNN QSKVLLFISH NTSDGEWHFV EVIFAEAVTL TLIDDSCKEK CIAKAPTPLE SDQSICAFQN SFLGGLPVGM TSNGVALLNF YNMPSTPSFV GCLQDIKIDW NHITLENISS GSSLNVKAGC VRKDWCESQP CQSRGRCINL WLSYQCDCHR PYEGPNCLRE YVAGRFGQDD STGYVIFTLD ESYGDTISLS MFVRTLQPSG LLLALENSTY QYIRVWLERG RLAMLTPNSP KLVVKFVLND GNVHLISLKI KPYKIELYQS SQNLGFISAS TWKIEKGDVI YIGGLPDKQE TELNGGFFKG CIQDVRLNNQ NLEFFPNPTN NASLNPVLVN VTQGCAGDNS CKSNPCHNGG VCHSRWDDFS CSCPALTSGK ACEEVQWCGF SPCPHGAQCQ PVLQGFECIA NAVFNGQSGQ ILFRSNGNIT RELTNITFGF RTRDANVIIL HAEKEPEFLN ISIQDSRLFF QLQSGNSFYM LSLTSLQSVN DGTWHEVTLS MTDPLSQTSR WQMEVDNETP FVTSTIATGS LNFLKDNTDI YVGDRAIDNI KGLQGCLSTI EIGGIYLSYF ENVHGFINKP QEEQFLKIST NSVVTGCLQL NVCNSNPCLH GGNCEDIYSS YHCSCPLGWS GKHCELNIDE CFSNPCIHGN CSDRVAAYHC TCEPGYTGVN CEVDIDNCQS HQCANGATCI SHTNGYSCLC FGNFTGKFCR QSRLPSTVCG NEKTNLTCYN GGNCTEFQTE LKCMCRPGFT GEWCEKDIDE CASDPCVNGG LCQDLLNKFQ CLCDVAFAGE RCEVDLADDL ISDIFTTIGS VTVALLLILL LAIVASVVTS NKRATQGTYS PSRQEKEGSR VEMWNLMPPP AMERLI